| Crystal structure of an Fab fragment in complex with a meningococcal serosubtype antigen and a protein G domain. | |
| | |
MedLine Citation:
|
PMID: 10512717 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
|
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. |
| | |
Authors:
|
J P Derrick; M C Maiden; I M Feavers |
Related Documents
:
|
6804187 - Studies on structural units of human monoclonal immunoglobulins. 18952827 - O-fucosylation of an antibody light chain: characterization of a modification occurring... 10986287 - Silk fibroin of bombyx mori is secreted, assembling a high molecular mass elementary un... 10318827 - Molecular cloning and tissue-specific expression of a novel murine laminin gamma3 chain. 8643107 - Fine chemical modifications at n- and c-termini enhance peptide presentation to t cells... 8940117 - Peptide g, containing the binding site of the 67-kda laminin receptor, increases and st... |
Publication Detail:
|
Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
|
Title: Journal of molecular biology Volume: 293 ISSN: 0022-2836 ISO Abbreviation: J. Mol. Biol. Publication Date: 1999 Oct |
Date Detail:
|
Created Date: 1999-11-22 Completed Date: 1999-11-22 Revised Date: 2011-08-01 |
Medline Journal Info:
|
Nlm Unique ID: 2985088R Medline TA: J Mol Biol Country: ENGLAND |
Other Details:
|
Languages: eng Pagination: 81-91 Citation Subset: IM |
Copyright Information:
|
Copyright 1999 Academic Press. |
Affiliation:
|
Department of Biomolecular Sciences, UMIST, Manchester, M60 1QD, UK. Jeremy.Derrick@umist.ac.uk |
| Data Bank Information | |
Bank Name/Acc. No.:
|
PDB/1QKZ |
Export Citation:
|
APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
|
Amino Acid Sequence Animals Antibodies, Monoclonal / chemistry*, immunology Antigenic Variation Antigens, Bacterial / chemistry Binding Sites Crystallography, X-Ray Hydrogen Bonding Immunoglobulin Fab Fragments / chemistry* Immunoglobulin Heavy Chains / chemistry Immunoglobulin Light Chains / chemistry Immunoglobulin Variable Region / chemistry Mice Models, Molecular Molecular Sequence Data Neisseria meningitidis / immunology* Nerve Tissue Proteins / chemistry*, immunology Porins / chemistry* Protein Structure, Secondary Sequence Alignment |
| Grant Support | |
ID/Acronym/Agency:
|
//Wellcome Trust |
| Chemical | |
Reg. No./Substance:
|
0/Antibodies, Monoclonal; 0/Antigens, Bacterial; 0/G-substrate; 0/Immunoglobulin Fab Fragments; 0/Immunoglobulin Heavy Chains; 0/Immunoglobulin Light Chains; 0/Immunoglobulin Variable Region; 0/MOPC21 monoclonal antibody; 0/Nerve Tissue Proteins; 0/Porins; 0/porin protein, Neisseria |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
Previous Document: Folding and association of the antibody domain CH3: prolyl isomerization preceeds dimerization.
Next Document: Structure of the complex of the antistasin-type inhibitor bdellastasin with trypsin and modelling of...