Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins
Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, ass...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
Garlatti, Virginie [verfasserIn] Belloy, Nicolas [verfasserIn] Martin, Lydie [verfasserIn] Lacroix, Monique [verfasserIn] Matsushita, Misao [verfasserIn] Endo, Yuichi [verfasserIn] Fujita, Teizo [verfasserIn] Fontecilla‐Camps, Juan Carlos [verfasserIn] Arlaud, Gérard J [verfasserIn] Thielens, Nicole M [verfasserIn] Gaboriaud, Christine [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2007 |
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| Schlagwörter: |
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| Anmerkung: |
© European Molecular Biology Organization 2007 |
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| Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 26(2007), 2 vom: 11. Jan., Seite 623-633 |
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| Übergeordnetes Werk: |
volume:26 ; year:2007 ; number:2 ; day:11 ; month:01 ; pages:623-633 |
| Links: |
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| DOI / URN: |
10.1038/sj.emboj.7601500 |
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| Katalog-ID: |
SPR057898162 |
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| 041 | |a eng | ||
| 100 | 1 | |a Garlatti, Virginie |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins |
| 264 | 1 | |c 2007 | |
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| 500 | |a © European Molecular Biology Organization 2007 | ||
| 520 | |a Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. | ||
| 650 | 4 | |a carbohydrate recognition |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a fibrinogen‐like domain |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a innate immunity |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a N‐acetyl group |7 (dpeaa)DE-He213 | |
| 650 | 4 | |a X‐ray crystallography |7 (dpeaa)DE-He213 | |
| 700 | 1 | |a Belloy, Nicolas |e verfasserin |4 aut | |
| 700 | 1 | |a Martin, Lydie |e verfasserin |4 aut | |
| 700 | 1 | |a Lacroix, Monique |e verfasserin |4 aut | |
| 700 | 1 | |a Matsushita, Misao |e verfasserin |4 aut | |
| 700 | 1 | |a Endo, Yuichi |e verfasserin |4 aut | |
| 700 | 1 | |a Fujita, Teizo |e verfasserin |4 aut | |
| 700 | 1 | |a Fontecilla‐Camps, Juan Carlos |e verfasserin |4 aut | |
| 700 | 1 | |a Arlaud, Gérard J |e verfasserin |4 aut | |
| 700 | 1 | |a Thielens, Nicole M |e verfasserin |4 aut | |
| 700 | 1 | |a Gaboriaud, Christine |e verfasserin |4 aut | |
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| 773 | 1 | 8 | |g volume:26 |g year:2007 |g number:2 |g day:11 |g month:01 |g pages:623-633 |
| 856 | 4 | 0 | |u https://dx.doi.org/10.1038/sj.emboj.7601500 |m X:SPRINGER |x Resolving-System |z lizenzpflichtig |3 Volltext |
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| 912 | |a GBV_ILN_602 | ||
| 912 | |a GBV_ILN_636 | ||
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| 912 | |a GBV_ILN_2001 | ||
| 912 | |a GBV_ILN_2003 | ||
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| 912 | |a GBV_ILN_2005 | ||
| 912 | |a GBV_ILN_2006 | ||
| 912 | |a GBV_ILN_2007 | ||
| 912 | |a GBV_ILN_2008 | ||
| 912 | |a GBV_ILN_2009 | ||
| 912 | |a GBV_ILN_2010 | ||
| 912 | |a GBV_ILN_2011 | ||
| 912 | |a GBV_ILN_2014 | ||
| 912 | |a GBV_ILN_2015 | ||
| 912 | |a GBV_ILN_2018 | ||
| 912 | |a GBV_ILN_2020 | ||
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| 912 | |a GBV_ILN_2025 | ||
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| 912 | |a GBV_ILN_2034 | ||
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| 912 | |a GBV_ILN_2038 | ||
| 912 | |a GBV_ILN_2044 | ||
| 912 | |a GBV_ILN_2048 | ||
| 912 | |a GBV_ILN_2049 | ||
| 912 | |a GBV_ILN_2050 | ||
| 912 | |a GBV_ILN_2055 | ||
| 912 | |a GBV_ILN_2056 | ||
| 912 | |a GBV_ILN_2057 | ||
| 912 | |a GBV_ILN_2059 | ||
| 912 | |a GBV_ILN_2061 | ||
| 912 | |a GBV_ILN_2064 | ||
| 912 | |a GBV_ILN_2068 | ||
| 912 | |a GBV_ILN_2088 | ||
| 912 | |a GBV_ILN_2093 | ||
| 912 | |a GBV_ILN_2106 | ||
| 912 | |a GBV_ILN_2108 | ||
| 912 | |a GBV_ILN_2110 | ||
| 912 | |a GBV_ILN_2111 | ||
| 912 | |a GBV_ILN_2113 | ||
| 912 | |a GBV_ILN_2118 | ||
| 912 | |a GBV_ILN_2119 | ||
| 912 | |a GBV_ILN_2122 | ||
| 912 | |a GBV_ILN_2129 | ||
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| 912 | |a GBV_ILN_2144 | ||
| 912 | |a GBV_ILN_2147 | ||
| 912 | |a GBV_ILN_2148 | ||
| 912 | |a GBV_ILN_2152 | ||
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| 912 | |a GBV_ILN_2470 | ||
| 912 | |a GBV_ILN_2472 | ||
| 912 | |a GBV_ILN_2507 | ||
| 912 | |a GBV_ILN_2522 | ||
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| 912 | |a GBV_ILN_4012 | ||
| 912 | |a GBV_ILN_4029 | ||
| 912 | |a GBV_ILN_4035 | ||
| 912 | |a GBV_ILN_4037 | ||
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| 912 | |a GBV_ILN_4112 | ||
| 912 | |a GBV_ILN_4125 | ||
| 912 | |a GBV_ILN_4126 | ||
| 912 | |a GBV_ILN_4155 | ||
| 912 | |a GBV_ILN_4242 | ||
| 912 | |a GBV_ILN_4246 | ||
| 912 | |a GBV_ILN_4249 | ||
| 912 | |a GBV_ILN_4251 | ||
| 912 | |a GBV_ILN_4305 | ||
| 912 | |a GBV_ILN_4306 | ||
| 912 | |a GBV_ILN_4307 | ||
| 912 | |a GBV_ILN_4313 | ||
| 912 | |a GBV_ILN_4322 | ||
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| 912 | |a GBV_ILN_4324 | ||
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| 912 | |a GBV_ILN_4328 | ||
| 912 | |a GBV_ILN_4333 | ||
| 912 | |a GBV_ILN_4334 | ||
| 912 | |a GBV_ILN_4335 | ||
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| 912 | |a GBV_ILN_4367 | ||
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| 951 | |a AR | ||
| 952 | |d 26 |j 2007 |e 2 |b 11 |c 01 |h 623-633 | ||
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2007 |
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2007 |
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10.1038/sj.emboj.7601500 doi (DE-627)SPR057898162 (SPR)sj.emboj.7601500-e DE-627 ger DE-627 rakwb eng Garlatti, Virginie verfasserin aut Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2007 Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. carbohydrate recognition (dpeaa)DE-He213 fibrinogen‐like domain (dpeaa)DE-He213 innate immunity (dpeaa)DE-He213 N‐acetyl group (dpeaa)DE-He213 X‐ray crystallography (dpeaa)DE-He213 Belloy, Nicolas verfasserin aut Martin, Lydie verfasserin aut Lacroix, Monique verfasserin aut Matsushita, Misao verfasserin aut Endo, Yuichi verfasserin aut Fujita, Teizo verfasserin aut Fontecilla‐Camps, Juan Carlos verfasserin aut Arlaud, Gérard J verfasserin aut Thielens, Nicole M verfasserin aut Gaboriaud, Christine verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 26(2007), 2 vom: 11. Jan., Seite 623-633 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:26 year:2007 number:2 day:11 month:01 pages:623-633 https://dx.doi.org/10.1038/sj.emboj.7601500 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 26 2007 2 11 01 623-633 |
| spelling |
10.1038/sj.emboj.7601500 doi (DE-627)SPR057898162 (SPR)sj.emboj.7601500-e DE-627 ger DE-627 rakwb eng Garlatti, Virginie verfasserin aut Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2007 Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. carbohydrate recognition (dpeaa)DE-He213 fibrinogen‐like domain (dpeaa)DE-He213 innate immunity (dpeaa)DE-He213 N‐acetyl group (dpeaa)DE-He213 X‐ray crystallography (dpeaa)DE-He213 Belloy, Nicolas verfasserin aut Martin, Lydie verfasserin aut Lacroix, Monique verfasserin aut Matsushita, Misao verfasserin aut Endo, Yuichi verfasserin aut Fujita, Teizo verfasserin aut Fontecilla‐Camps, Juan Carlos verfasserin aut Arlaud, Gérard J verfasserin aut Thielens, Nicole M verfasserin aut Gaboriaud, Christine verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 26(2007), 2 vom: 11. Jan., Seite 623-633 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:26 year:2007 number:2 day:11 month:01 pages:623-633 https://dx.doi.org/10.1038/sj.emboj.7601500 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 26 2007 2 11 01 623-633 |
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10.1038/sj.emboj.7601500 doi (DE-627)SPR057898162 (SPR)sj.emboj.7601500-e DE-627 ger DE-627 rakwb eng Garlatti, Virginie verfasserin aut Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2007 Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. carbohydrate recognition (dpeaa)DE-He213 fibrinogen‐like domain (dpeaa)DE-He213 innate immunity (dpeaa)DE-He213 N‐acetyl group (dpeaa)DE-He213 X‐ray crystallography (dpeaa)DE-He213 Belloy, Nicolas verfasserin aut Martin, Lydie verfasserin aut Lacroix, Monique verfasserin aut Matsushita, Misao verfasserin aut Endo, Yuichi verfasserin aut Fujita, Teizo verfasserin aut Fontecilla‐Camps, Juan Carlos verfasserin aut Arlaud, Gérard J verfasserin aut Thielens, Nicole M verfasserin aut Gaboriaud, Christine verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 26(2007), 2 vom: 11. Jan., Seite 623-633 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:26 year:2007 number:2 day:11 month:01 pages:623-633 https://dx.doi.org/10.1038/sj.emboj.7601500 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 26 2007 2 11 01 623-633 |
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10.1038/sj.emboj.7601500 doi (DE-627)SPR057898162 (SPR)sj.emboj.7601500-e DE-627 ger DE-627 rakwb eng Garlatti, Virginie verfasserin aut Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2007 Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. carbohydrate recognition (dpeaa)DE-He213 fibrinogen‐like domain (dpeaa)DE-He213 innate immunity (dpeaa)DE-He213 N‐acetyl group (dpeaa)DE-He213 X‐ray crystallography (dpeaa)DE-He213 Belloy, Nicolas verfasserin aut Martin, Lydie verfasserin aut Lacroix, Monique verfasserin aut Matsushita, Misao verfasserin aut Endo, Yuichi verfasserin aut Fujita, Teizo verfasserin aut Fontecilla‐Camps, Juan Carlos verfasserin aut Arlaud, Gérard J verfasserin aut Thielens, Nicole M verfasserin aut Gaboriaud, Christine verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 26(2007), 2 vom: 11. Jan., Seite 623-633 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:26 year:2007 number:2 day:11 month:01 pages:623-633 https://dx.doi.org/10.1038/sj.emboj.7601500 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 26 2007 2 11 01 623-633 |
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10.1038/sj.emboj.7601500 doi (DE-627)SPR057898162 (SPR)sj.emboj.7601500-e DE-627 ger DE-627 rakwb eng Garlatti, Virginie verfasserin aut Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins 2007 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2007 Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. carbohydrate recognition (dpeaa)DE-He213 fibrinogen‐like domain (dpeaa)DE-He213 innate immunity (dpeaa)DE-He213 N‐acetyl group (dpeaa)DE-He213 X‐ray crystallography (dpeaa)DE-He213 Belloy, Nicolas verfasserin aut Martin, Lydie verfasserin aut Lacroix, Monique verfasserin aut Matsushita, Misao verfasserin aut Endo, Yuichi verfasserin aut Fujita, Teizo verfasserin aut Fontecilla‐Camps, Juan Carlos verfasserin aut Arlaud, Gérard J verfasserin aut Thielens, Nicole M verfasserin aut Gaboriaud, Christine verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 26(2007), 2 vom: 11. Jan., Seite 623-633 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:26 year:2007 number:2 day:11 month:01 pages:623-633 https://dx.doi.org/10.1038/sj.emboj.7601500 X:SPRINGER Resolving-System lizenzpflichtig Volltext SYSFLAG_0 GBV_SPRINGER GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_72 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_168 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_252 GBV_ILN_266 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2018 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2113 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2190 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4012 GBV_ILN_4029 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4155 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4328 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 26 2007 2 11 01 623-633 |
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Enthalten in The EMBO Journal 26(2007), 2 vom: 11. Jan., Seite 623-633 volume:26 year:2007 number:2 day:11 month:01 pages:623-633 |
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Garlatti, Virginie @@aut@@ Belloy, Nicolas @@aut@@ Martin, Lydie @@aut@@ Lacroix, Monique @@aut@@ Matsushita, Misao @@aut@@ Endo, Yuichi @@aut@@ Fujita, Teizo @@aut@@ Fontecilla‐Camps, Juan Carlos @@aut@@ Arlaud, Gérard J @@aut@@ Thielens, Nicole M @@aut@@ Gaboriaud, Christine @@aut@@ |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000naa a22002652 4500</leader><controlfield tag="001">SPR057898162</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20241019064905.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">241019s2007 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1038/sj.emboj.7601500</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR057898162</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)sj.emboj.7601500-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Garlatti, Virginie</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2007</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© European Molecular Biology Organization 2007</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. 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Garlatti, Virginie |
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Garlatti, Virginie misc carbohydrate recognition misc fibrinogen‐like domain misc innate immunity misc N‐acetyl group misc X‐ray crystallography Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins |
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Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins carbohydrate recognition (dpeaa)DE-He213 fibrinogen‐like domain (dpeaa)DE-He213 innate immunity (dpeaa)DE-He213 N‐acetyl group (dpeaa)DE-He213 X‐ray crystallography (dpeaa)DE-He213 |
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Garlatti, Virginie Belloy, Nicolas Martin, Lydie Lacroix, Monique Matsushita, Misao Endo, Yuichi Fujita, Teizo Fontecilla‐Camps, Juan Carlos Arlaud, Gérard J Thielens, Nicole M Gaboriaud, Christine |
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structural insights into the innate immune recognition specificities of l‐ and h‐ficolins |
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Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins |
| abstract |
Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. © European Molecular Biology Organization 2007 |
| abstractGer |
Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. © European Molecular Biology Organization 2007 |
| abstract_unstemmed |
Abstract Innate immunity relies critically upon the ability of a few pattern recognition molecules to sense molecular markers on pathogens, but little is known about these interactions at the atomic level. Human L‐ and H‐ficolins are soluble oligomeric defence proteins with lectin‐like activity, assembled from collagen fibers prolonged by fibrinogen‐like recognition domains. The X‐ray structures of their trimeric recognition domains, alone and in complex with various ligands, have been solved to resolutions up to 1.95 and 1.7 Å, respectively. Both domains have three‐lobed structures with clefts separating the distal parts of the protomers. $ Ca^{2+} $ ions are found at sites homologous to those described for tachylectin 5A (TL5A), an invertebrate lectin. Outer binding sites (S1) homologous to the GlcNAc‐binding pocket of TL5A are present in the ficolins but show different structures and specificities. In L‐ficolin, three additional binding sites (S2–S4) surround the cleft. Together, they define an unpredicted continuous recognition surface able to sense various acetylated and neutral carbohydrate markers in the context of extended polysaccharides such as 1,3‐β‐D‐glucan, as found on microbial or apoptotic surfaces. © European Molecular Biology Organization 2007 |
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2 |
| title_short |
Structural insights into the innate immune recognition specificities of L‐ and H‐ficolins |
| url |
https://dx.doi.org/10.1038/sj.emboj.7601500 |
| remote_bool |
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| author2 |
Belloy, Nicolas Martin, Lydie Lacroix, Monique Matsushita, Misao Endo, Yuichi Fujita, Teizo Fontecilla‐Camps, Juan Carlos Arlaud, Gérard J Thielens, Nicole M Gaboriaud, Christine |
| author2Str |
Belloy, Nicolas Martin, Lydie Lacroix, Monique Matsushita, Misao Endo, Yuichi Fujita, Teizo Fontecilla‐Camps, Juan Carlos Arlaud, Gérard J Thielens, Nicole M Gaboriaud, Christine |
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| doi_str |
10.1038/sj.emboj.7601500 |
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2024-10-19T04:51:34.407Z |
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| score |
7.399748 |