Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b
Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address t...
Ausführliche Beschreibung
Autor*in: |
Garcia‐Alles, Luis F [verfasserIn] Versluis, Kees [verfasserIn] Maveyraud, Laurent [verfasserIn] Vallina, Ana Tesouro [verfasserIn] Sansano, Sebastiano [verfasserIn] Bello, Nana Fatimath [verfasserIn] Gober, Hans‐Jürgen [verfasserIn] Guillet, Valérie [verfasserIn] de la Salle, Henri [verfasserIn] Puzo, Germain [verfasserIn] Mori, Lucia [verfasserIn] Heck, Albert JR [verfasserIn] De Libero, Gennaro [verfasserIn] Mourey, Lionel [verfasserIn] |
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E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2006 |
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Anmerkung: |
© European Molecular Biology Organization 2006 |
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Übergeordnetes Werk: |
Enthalten in: The EMBO Journal - Nature Publishing Group UK, 2023, 25(2006), 15 vom: 27. Juli, Seite 3684-3692 |
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Übergeordnetes Werk: |
volume:25 ; year:2006 ; number:15 ; day:27 ; month:07 ; pages:3684-3692 |
Links: |
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DOI / URN: |
10.1038/sj.emboj.7601244 |
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Katalog-ID: |
SPR057897700 |
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245 | 1 | 0 | |a Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b |
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520 | |a Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. | ||
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650 | 4 | |a endogenous lipid |7 (dpeaa)DE-He213 | |
650 | 4 | |a mass spectrometry |7 (dpeaa)DE-He213 | |
700 | 1 | |a Versluis, Kees |e verfasserin |4 aut | |
700 | 1 | |a Maveyraud, Laurent |e verfasserin |4 aut | |
700 | 1 | |a Vallina, Ana Tesouro |e verfasserin |4 aut | |
700 | 1 | |a Sansano, Sebastiano |e verfasserin |4 aut | |
700 | 1 | |a Bello, Nana Fatimath |e verfasserin |4 aut | |
700 | 1 | |a Gober, Hans‐Jürgen |e verfasserin |4 aut | |
700 | 1 | |a Guillet, Valérie |e verfasserin |4 aut | |
700 | 1 | |a de la Salle, Henri |e verfasserin |4 aut | |
700 | 1 | |a Puzo, Germain |e verfasserin |4 aut | |
700 | 1 | |a Mori, Lucia |e verfasserin |4 aut | |
700 | 1 | |a Heck, Albert JR |e verfasserin |4 aut | |
700 | 1 | |a De Libero, Gennaro |e verfasserin |4 aut | |
700 | 1 | |a Mourey, Lionel |e verfasserin |4 aut | |
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2006 |
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10.1038/sj.emboj.7601244 doi (DE-627)SPR057897700 (SPR)sj.emboj.7601244-e DE-627 ger DE-627 rakwb eng Garcia‐Alles, Luis F verfasserin aut Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. antigen (dpeaa)DE-He213 CD1 proteins (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 endogenous lipid (dpeaa)DE-He213 mass spectrometry (dpeaa)DE-He213 Versluis, Kees verfasserin aut Maveyraud, Laurent verfasserin aut Vallina, Ana Tesouro verfasserin aut Sansano, Sebastiano verfasserin aut Bello, Nana Fatimath verfasserin aut Gober, Hans‐Jürgen verfasserin aut Guillet, Valérie verfasserin aut de la Salle, Henri verfasserin aut Puzo, Germain verfasserin aut Mori, Lucia verfasserin aut Heck, Albert JR verfasserin aut De Libero, Gennaro verfasserin aut Mourey, Lionel verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 15 vom: 27. Juli, Seite 3684-3692 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:15 day:27 month:07 pages:3684-3692 https://dx.doi.org/10.1038/sj.emboj.7601244 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 25 2006 15 27 07 3684-3692 |
spelling |
10.1038/sj.emboj.7601244 doi (DE-627)SPR057897700 (SPR)sj.emboj.7601244-e DE-627 ger DE-627 rakwb eng Garcia‐Alles, Luis F verfasserin aut Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. antigen (dpeaa)DE-He213 CD1 proteins (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 endogenous lipid (dpeaa)DE-He213 mass spectrometry (dpeaa)DE-He213 Versluis, Kees verfasserin aut Maveyraud, Laurent verfasserin aut Vallina, Ana Tesouro verfasserin aut Sansano, Sebastiano verfasserin aut Bello, Nana Fatimath verfasserin aut Gober, Hans‐Jürgen verfasserin aut Guillet, Valérie verfasserin aut de la Salle, Henri verfasserin aut Puzo, Germain verfasserin aut Mori, Lucia verfasserin aut Heck, Albert JR verfasserin aut De Libero, Gennaro verfasserin aut Mourey, Lionel verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 15 vom: 27. Juli, Seite 3684-3692 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:15 day:27 month:07 pages:3684-3692 https://dx.doi.org/10.1038/sj.emboj.7601244 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 25 2006 15 27 07 3684-3692 |
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10.1038/sj.emboj.7601244 doi (DE-627)SPR057897700 (SPR)sj.emboj.7601244-e DE-627 ger DE-627 rakwb eng Garcia‐Alles, Luis F verfasserin aut Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. antigen (dpeaa)DE-He213 CD1 proteins (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 endogenous lipid (dpeaa)DE-He213 mass spectrometry (dpeaa)DE-He213 Versluis, Kees verfasserin aut Maveyraud, Laurent verfasserin aut Vallina, Ana Tesouro verfasserin aut Sansano, Sebastiano verfasserin aut Bello, Nana Fatimath verfasserin aut Gober, Hans‐Jürgen verfasserin aut Guillet, Valérie verfasserin aut de la Salle, Henri verfasserin aut Puzo, Germain verfasserin aut Mori, Lucia verfasserin aut Heck, Albert JR verfasserin aut De Libero, Gennaro verfasserin aut Mourey, Lionel verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 15 vom: 27. Juli, Seite 3684-3692 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:15 day:27 month:07 pages:3684-3692 https://dx.doi.org/10.1038/sj.emboj.7601244 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 25 2006 15 27 07 3684-3692 |
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10.1038/sj.emboj.7601244 doi (DE-627)SPR057897700 (SPR)sj.emboj.7601244-e DE-627 ger DE-627 rakwb eng Garcia‐Alles, Luis F verfasserin aut Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. antigen (dpeaa)DE-He213 CD1 proteins (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 endogenous lipid (dpeaa)DE-He213 mass spectrometry (dpeaa)DE-He213 Versluis, Kees verfasserin aut Maveyraud, Laurent verfasserin aut Vallina, Ana Tesouro verfasserin aut Sansano, Sebastiano verfasserin aut Bello, Nana Fatimath verfasserin aut Gober, Hans‐Jürgen verfasserin aut Guillet, Valérie verfasserin aut de la Salle, Henri verfasserin aut Puzo, Germain verfasserin aut Mori, Lucia verfasserin aut Heck, Albert JR verfasserin aut De Libero, Gennaro verfasserin aut Mourey, Lionel verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 15 vom: 27. Juli, Seite 3684-3692 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:15 day:27 month:07 pages:3684-3692 https://dx.doi.org/10.1038/sj.emboj.7601244 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 25 2006 15 27 07 3684-3692 |
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10.1038/sj.emboj.7601244 doi (DE-627)SPR057897700 (SPR)sj.emboj.7601244-e DE-627 ger DE-627 rakwb eng Garcia‐Alles, Luis F verfasserin aut Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b 2006 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © European Molecular Biology Organization 2006 Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. antigen (dpeaa)DE-He213 CD1 proteins (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 endogenous lipid (dpeaa)DE-He213 mass spectrometry (dpeaa)DE-He213 Versluis, Kees verfasserin aut Maveyraud, Laurent verfasserin aut Vallina, Ana Tesouro verfasserin aut Sansano, Sebastiano verfasserin aut Bello, Nana Fatimath verfasserin aut Gober, Hans‐Jürgen verfasserin aut Guillet, Valérie verfasserin aut de la Salle, Henri verfasserin aut Puzo, Germain verfasserin aut Mori, Lucia verfasserin aut Heck, Albert JR verfasserin aut De Libero, Gennaro verfasserin aut Mourey, Lionel verfasserin aut Enthalten in The EMBO Journal Nature Publishing Group UK, 2023 25(2006), 15 vom: 27. Juli, Seite 3684-3692 (DE-627)266022529 (DE-600)1467419-1 1460-2075 nnns volume:25 year:2006 number:15 day:27 month:07 pages:3684-3692 https://dx.doi.org/10.1038/sj.emboj.7601244 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 25 2006 15 27 07 3684-3692 |
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Enthalten in The EMBO Journal 25(2006), 15 vom: 27. Juli, Seite 3684-3692 volume:25 year:2006 number:15 day:27 month:07 pages:3684-3692 |
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Garcia‐Alles, Luis F @@aut@@ Versluis, Kees @@aut@@ Maveyraud, Laurent @@aut@@ Vallina, Ana Tesouro @@aut@@ Sansano, Sebastiano @@aut@@ Bello, Nana Fatimath @@aut@@ Gober, Hans‐Jürgen @@aut@@ Guillet, Valérie @@aut@@ de la Salle, Henri @@aut@@ Puzo, Germain @@aut@@ Mori, Lucia @@aut@@ Heck, Albert JR @@aut@@ De Libero, Gennaro @@aut@@ Mourey, Lionel @@aut@@ |
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The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. 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|
author |
Garcia‐Alles, Luis F |
spellingShingle |
Garcia‐Alles, Luis F misc antigen misc CD1 proteins misc crystal structure misc endogenous lipid misc mass spectrometry Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b |
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Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b antigen (dpeaa)DE-He213 CD1 proteins (dpeaa)DE-He213 crystal structure (dpeaa)DE-He213 endogenous lipid (dpeaa)DE-He213 mass spectrometry (dpeaa)DE-He213 |
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misc antigen misc CD1 proteins misc crystal structure misc endogenous lipid misc mass spectrometry |
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misc antigen misc CD1 proteins misc crystal structure misc endogenous lipid misc mass spectrometry |
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Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b |
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Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b |
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Garcia‐Alles, Luis F |
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Garcia‐Alles, Luis F Versluis, Kees Maveyraud, Laurent Vallina, Ana Tesouro Sansano, Sebastiano Bello, Nana Fatimath Gober, Hans‐Jürgen Guillet, Valérie de la Salle, Henri Puzo, Germain Mori, Lucia Heck, Albert JR De Libero, Gennaro Mourey, Lionel |
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Garcia‐Alles, Luis F |
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10.1038/sj.emboj.7601244 |
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verfasserin |
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endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of cd1b |
title_auth |
Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b |
abstract |
Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. © European Molecular Biology Organization 2006 |
abstractGer |
Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. © European Molecular Biology Organization 2006 |
abstract_unstemmed |
Abstract CD1 proteins present lipid antigens to T cells. The antigens are acquired in the endosomal compartments. This raises the question of how the large hydrophobic CD1 pockets are preserved between the moment of biosynthesis in the endoplasmic reticulum and arrival to the endosomes. To address this issue, the natural ligands associated with a soluble form of human CD1b have been investigated. Using isoelectric focusing, native mass spectrometry and resolving the crystal structure at 1.8 Å resolution, we found that human CD1b is simultaneously associated with endogenous phosphatidylcholine (PC) and a 41–44 carbon atoms‐long spacer molecule. The two lipids appear to work in concert to stabilize the CD1b groove, their combined size slightly exceeding the maximal groove capacity. We propose that the spacer serves to prevent binding of ligands with long lipid tails, whereas short‐chain lipids might still displace the PC, which is exposed at the groove entrance. The data presented herein explain how the CD1b groove is preserved, and provide a rationale for the in vivo antigen‐binding properties of CD1b. © European Molecular Biology Organization 2006 |
collection_details |
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container_issue |
15 |
title_short |
Endogenous phosphatidylcholine and a long spacer ligand stabilize the lipid‐binding groove of CD1b |
url |
https://dx.doi.org/10.1038/sj.emboj.7601244 |
remote_bool |
true |
author2 |
Versluis, Kees Maveyraud, Laurent Vallina, Ana Tesouro Sansano, Sebastiano Bello, Nana Fatimath Gober, Hans‐Jürgen Guillet, Valérie de la Salle, Henri Puzo, Germain Mori, Lucia Heck, Albert JR De Libero, Gennaro Mourey, Lionel |
author2Str |
Versluis, Kees Maveyraud, Laurent Vallina, Ana Tesouro Sansano, Sebastiano Bello, Nana Fatimath Gober, Hans‐Jürgen Guillet, Valérie de la Salle, Henri Puzo, Germain Mori, Lucia Heck, Albert JR De Libero, Gennaro Mourey, Lionel |
ppnlink |
266022529 |
mediatype_str_mv |
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hochschulschrift_bool |
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doi_str |
10.1038/sj.emboj.7601244 |
up_date |
2024-10-19T04:52:10.553Z |
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1813316664619433984 |
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score |
7.4022093 |