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1qkz
From Proteopedia
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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''' | '''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''' | ||
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[[Category: Feavers, I.]] | [[Category: Feavers, I.]] | ||
[[Category: Maiden, M C.J.]] | [[Category: Maiden, M C.J.]] | ||
| - | [[Category: | + | [[Category: Fab]] |
| - | [[Category: | + | [[Category: Neisseria meningitidi]] |
| - | [[Category: | + | [[Category: Pora]] |
| - | [[Category: | + | [[Category: Porin]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:24:03 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:24, 3 May 2008
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 Streptococcus. 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 Page seeded by OCA on Sat May 3 06:24:03 2008
