Epitopes described in "Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide."

Reference
Article Authors:L J Stern; J H Brown; T S Jardetzky; J C Gorga; R G Urban; J L Strominger; D C Wiley
Article Title:Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide.
Reference Detail
Reference ID:315104
Abstract:An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.
Affiliations:Department of Biochemistry and Molecular Biology, Harvard University, Cambridge Massachusetts 62138.
Date:1994
Reference Type:Literature
PubMed ID:8145819
Journal:Nature
Journal Volume:368
Article Pages:215-21
Journal ISSN:1476-4687
Article Chemical List:HLA-DR1 Antigen;Hemagglutinin Glycoproteins, Influenza Virus;Hemagglutinins;Hemagglutinins, Viral;Peptide Fragments;Receptors, Antigen, T-Cell;influenza hemagglutinin (306-318)
Article MeSH List:Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; HLA-DR1 Antigen(chemistry; metabolism); Hemagglutinin Glycoproteins, Influenza Virus; Hemagglutinins(chemistry); Hemagglutinins, Viral(chemistry); Humans; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Peptide Fragments(chemistry); Protein Binding; Protein Conformation; Receptors, Antigen, T-Cell(metabolism)
Article Comments:Data originally imported from the Database of Functional Molecular Immunology, FIMM (http://sdmc.lit.org.sg:8080/fimm/)
Curation Last Updated:2013-05-28 20:10:11