Structure of a $ V_{H} $H isolated from a naïve phage display library
Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnolog...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
White, Brandy [verfasserIn] |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2019 |
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| Schlagwörter: |
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| Anmerkung: |
© The Author(s) 2019 |
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| Übergeordnetes Werk: |
Enthalten in: BMC Research Notes - London, 2008, 12(2019), 1 vom: 19. März |
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| Übergeordnetes Werk: |
volume:12 ; year:2019 ; number:1 ; day:19 ; month:03 |
| Links: |
|---|
| DOI / URN: |
10.1186/s13104-019-4197-0 |
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| Katalog-ID: |
SPR030339987 |
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| 245 | 1 | 0 | |a Structure of a $ V_{H} $H isolated from a naïve phage display library |
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| 520 | |a Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. | ||
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10.1186/s13104-019-4197-0 doi (DE-627)SPR030339987 (SPR)s13104-019-4197-0-e DE-627 ger DE-627 rakwb eng White, Brandy verfasserin aut Structure of a $ V_{H} $H isolated from a naïve phage display library 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. Nanobody (dpeaa)DE-He213 V (dpeaa)DE-He213 H (dpeaa)DE-He213 Single domain antibody (dpeaa)DE-He213 Huh, Ian aut Brooks, Cory L. (orcid)0000-0002-6745-6526 aut Enthalten in BMC Research Notes London, 2008 12(2019), 1 vom: 19. März (DE-627)559431805 (DE-600)2413336-X 1756-0500 nnns volume:12 year:2019 number:1 day:19 month:03 https://dx.doi.org/10.1186/s13104-019-4197-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 19 03 |
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10.1186/s13104-019-4197-0 doi (DE-627)SPR030339987 (SPR)s13104-019-4197-0-e DE-627 ger DE-627 rakwb eng White, Brandy verfasserin aut Structure of a $ V_{H} $H isolated from a naïve phage display library 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. Nanobody (dpeaa)DE-He213 V (dpeaa)DE-He213 H (dpeaa)DE-He213 Single domain antibody (dpeaa)DE-He213 Huh, Ian aut Brooks, Cory L. (orcid)0000-0002-6745-6526 aut Enthalten in BMC Research Notes London, 2008 12(2019), 1 vom: 19. März (DE-627)559431805 (DE-600)2413336-X 1756-0500 nnns volume:12 year:2019 number:1 day:19 month:03 https://dx.doi.org/10.1186/s13104-019-4197-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 19 03 |
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10.1186/s13104-019-4197-0 doi (DE-627)SPR030339987 (SPR)s13104-019-4197-0-e DE-627 ger DE-627 rakwb eng White, Brandy verfasserin aut Structure of a $ V_{H} $H isolated from a naïve phage display library 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. Nanobody (dpeaa)DE-He213 V (dpeaa)DE-He213 H (dpeaa)DE-He213 Single domain antibody (dpeaa)DE-He213 Huh, Ian aut Brooks, Cory L. (orcid)0000-0002-6745-6526 aut Enthalten in BMC Research Notes London, 2008 12(2019), 1 vom: 19. März (DE-627)559431805 (DE-600)2413336-X 1756-0500 nnns volume:12 year:2019 number:1 day:19 month:03 https://dx.doi.org/10.1186/s13104-019-4197-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 19 03 |
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10.1186/s13104-019-4197-0 doi (DE-627)SPR030339987 (SPR)s13104-019-4197-0-e DE-627 ger DE-627 rakwb eng White, Brandy verfasserin aut Structure of a $ V_{H} $H isolated from a naïve phage display library 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. Nanobody (dpeaa)DE-He213 V (dpeaa)DE-He213 H (dpeaa)DE-He213 Single domain antibody (dpeaa)DE-He213 Huh, Ian aut Brooks, Cory L. (orcid)0000-0002-6745-6526 aut Enthalten in BMC Research Notes London, 2008 12(2019), 1 vom: 19. März (DE-627)559431805 (DE-600)2413336-X 1756-0500 nnns volume:12 year:2019 number:1 day:19 month:03 https://dx.doi.org/10.1186/s13104-019-4197-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 19 03 |
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10.1186/s13104-019-4197-0 doi (DE-627)SPR030339987 (SPR)s13104-019-4197-0-e DE-627 ger DE-627 rakwb eng White, Brandy verfasserin aut Structure of a $ V_{H} $H isolated from a naïve phage display library 2019 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Author(s) 2019 Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. Nanobody (dpeaa)DE-He213 V (dpeaa)DE-He213 H (dpeaa)DE-He213 Single domain antibody (dpeaa)DE-He213 Huh, Ian aut Brooks, Cory L. (orcid)0000-0002-6745-6526 aut Enthalten in BMC Research Notes London, 2008 12(2019), 1 vom: 19. März (DE-627)559431805 (DE-600)2413336-X 1756-0500 nnns volume:12 year:2019 number:1 day:19 month:03 https://dx.doi.org/10.1186/s13104-019-4197-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 12 2019 1 19 03 |
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Structure of a $ V_{H} $H isolated from a naïve phage display library Nanobody (dpeaa)DE-He213 V (dpeaa)DE-He213 H (dpeaa)DE-He213 Single domain antibody (dpeaa)DE-He213 |
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structure of a $ v_{h} $h isolated from a naïve phage display library |
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Structure of a $ V_{H} $H isolated from a naïve phage display library |
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Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. © The Author(s) 2019 |
| abstractGer |
Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. © The Author(s) 2019 |
| abstract_unstemmed |
Objective To determine the X-ray structure and biophysical properties of a Camelid $ V_{H} $H isolated from a naïve phage display library. Results Single domain antibodies ($ V_{H} $H) derived from the unique immune system of the Camelidae family have gained traction as useful tools for biotechnology as well as a source of potentially novel therapeutics. Here we report the structure and biophysical characterization of a $ V_{H} $H originally isolated from a naïve camelid phage display library. $ V_{H} $H R419 has a melting temperate of 66 °C and was found to be a monomer in solution. The protein crystallized in space group P$ 6_{5} $22 and the structure was solved by molecular replacement to a resolution of 1.5 Å. The structure revealed a flat paratope with CDR loops that could be classified into existing canonical loop structures. A combination of high expression yield, stability and rapid crystallization might make R419 into a candidate scaffold for CDR grafting and homology modeling. © The Author(s) 2019 |
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| score |
7.400981 |