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1QKZ

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

Summary for 1QKZ
Entry DOI10.2210/pdb1qkz/pdb
DescriptorPROTEIN G-PRIME, ANTIBODY, MAJOR OUTER MEMBRANE PROTEIN P1.16, ... (5 entities in total)
Functional Keywordsimmune system, fab, pora, neisseria meningitidis, porin
Biological sourceSTREPTOCOCCUS SP.
More
Total number of polymer chains4
Total formula weight55611.86
Authors
Derrick, J.P.,Feavers, I.,Maiden, M.C.J. (deposition date: 1999-08-17, release date: 2000-02-06, Last modification date: 2024-11-20)
Primary citationDerrick, J.P.,Feavers, I.M.,Maiden, M.C.J.
Crystal Structure of an Fab Fragment in Complex with a Meningococcal Serosubtype Antigen and a Protein G Domain
J.Mol.Biol., 293:81-, 1999
Cited by
PubMed Abstract: 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.
PubMed: 10512717
DOI: 10.1006/JMBI.1999.3144
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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