1qkz
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qkz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qkz OCA], [http://www.ebi.ac.uk/pdbsum/1qkz PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qkz RCSB]</span> | ||
}} | }} | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QKZ is a [[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/ | + | 1QKZ is a [[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/Streptococcus Streptococcus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QKZ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Neisseria meningitidis]] | [[Category: Neisseria meningitidis]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: | + | [[Category: Streptococcus]] |
[[Category: Derrick, J P.]] | [[Category: Derrick, J P.]] | ||
[[Category: Feavers, I.]] | [[Category: Feavers, I.]] | ||
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[[Category: porin]] | [[Category: porin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:10 2008'' |
Revision as of 20:15, 30 March 2008
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| , resolution 1.95Å | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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