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1qkz
From Proteopedia
(New page: 200px<br /> <applet load="1qkz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qkz, resolution 1.95Å" /> '''FAB FRAGMENT (MN14C...) |
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| - | [[Image:1qkz.gif|left|200px]]<br /> | + | [[Image:1qkz.gif|left|200px]]<br /><applet load="1qkz" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1qkz" size=" | + | |
caption="1qkz, resolution 1.95Å" /> | caption="1qkz, resolution 1.95Å" /> | ||
'''FAB FRAGMENT (MN14C11.6) IN COMPLEX WITH A PEPTIDE ANTIGEN DERIVED FROM NEISSERIA MENINGITIDIS P1.7 SEROSUBTYPE ANTIGEN AND DOMAIN II FROM STREPTOCOCCAL PROTEIN G'''<br /> | '''FAB FRAGMENT (MN14C11.6) IN COMPLEX WITH A PEPTIDE ANTIGEN DERIVED FROM NEISSERIA MENINGITIDIS P1.7 SEROSUBTYPE ANTIGEN AND DOMAIN II FROM STREPTOCOCCAL PROTEIN G'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Many pathogens present highly variable surface proteins to their host as a | + | Many pathogens present highly variable surface proteins to their host as a means of evading immune responses. The structure of a peptide antigen corresponding to the subtype P1.7 variant of the porin PorA from the human pathogen Neisseria meningitidis was determined by solution of the X-ray crystal structure of the ternary complex of the peptide (ANGGASGQVK) in complex with a Fab fragment and a domain from streptococcal protein G to 1.95 A resolution. The peptide adopted a beta-hairpin structure with a type I beta-turn between residues Gly4P and Gly7P, the conformation of the peptide being further stabilised by a pair of hydrogen bonds from the side-chain of Asn2P to main-chain atoms in Val9P. The antigen binding site within the Fab formed a distinct crevice lined by a high proportion of apolar amino acids. Recognition was supplemented by hydrogen bonds from heavy chain residues Thr50H, Asp95H, Leu97H and Tyr100H to main-chain and side-chain atoms in the peptide. Complementarity-determining region (CDR) 3 of the heavy chain was responsible for approximately 50 % of the buried surface area formed by peptide-Fab binding, with the remainder made up from CDRs 1 and 3 of the light chain and CDRs 1 and 2 of the heavy chain. Knowledge of the structures of variable surface antigens such as PorA is an essential prerequisite to a molecular understanding of antigenic variation and its implications for vaccine design. |
==About this Structure== | ==About this Structure== | ||
| - | 1QKZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus], [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] and [http://en.wikipedia.org/wiki/Streptococcaceae Streptococcaceae]. Full crystallographic information is available from [http:// | + | 1QKZ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus], [http://en.wikipedia.org/wiki/Neisseria_meningitidis Neisseria meningitidis] and [http://en.wikipedia.org/wiki/Streptococcaceae Streptococcaceae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Streptococcaceae]] | [[Category: Streptococcaceae]] | ||
| - | [[Category: Derrick, J | + | [[Category: Derrick, J P.]] |
[[Category: Feavers, I.]] | [[Category: Feavers, I.]] | ||
| - | [[Category: Maiden, M | + | [[Category: Maiden, M C.J.]] |
[[Category: fab]] | [[Category: fab]] | ||
[[Category: neisseria meningitidis]] | [[Category: neisseria meningitidis]] | ||
| Line 24: | Line 23: | ||
[[Category: porin]] | [[Category: porin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:50 2008'' |
Revision as of 12:40, 21 February 2008
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FAB FRAGMENT (MN14C11.6) IN COMPLEX WITH A PEPTIDE ANTIGEN DERIVED FROM NEISSERIA MENINGITIDIS P1.7 SEROSUBTYPE ANTIGEN AND DOMAIN II FROM STREPTOCOCCAL PROTEIN G
Overview
Many pathogens present highly variable surface proteins to their host as a means of evading immune responses. The structure of a peptide antigen corresponding to the subtype P1.7 variant of the porin PorA from the human pathogen Neisseria meningitidis was determined by solution of the X-ray crystal structure of the ternary complex of the peptide (ANGGASGQVK) in complex with a Fab fragment and a domain from streptococcal protein G to 1.95 A resolution. The peptide adopted a beta-hairpin structure with a type I beta-turn between residues Gly4P and Gly7P, the conformation of the peptide being further stabilised by a pair of hydrogen bonds from the side-chain of Asn2P to main-chain atoms in Val9P. The antigen binding site within the Fab formed a distinct crevice lined by a high proportion of apolar amino acids. Recognition was supplemented by hydrogen bonds from heavy chain residues Thr50H, Asp95H, Leu97H and Tyr100H to main-chain and side-chain atoms in the peptide. Complementarity-determining region (CDR) 3 of the heavy chain was responsible for approximately 50 % of the buried surface area formed by peptide-Fab binding, with the remainder made up from CDRs 1 and 3 of the light chain and CDRs 1 and 2 of the heavy chain. Knowledge of the structures of variable surface antigens such as PorA is an essential prerequisite to a molecular understanding of antigenic variation and its implications for vaccine design.
About this Structure
1QKZ is a Protein complex structure of sequences from Mus musculus, Neisseria meningitidis and Streptococcaceae. Full crystallographic information is available from OCA.
Reference
Crystal structure of an Fab fragment in complex with a meningococcal serosubtype antigen and a protein G domain., Derrick JP, Maiden MC, Feavers IM, J Mol Biol. 1999 Oct 15;293(1):81-91. PMID:10512717
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