Epitopes described in "Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53."

Reference
Article Authors:K J Smith; S W Reid; K Harlos; A J McMichael; D I Stuart; J I Bell; E Y Jones
Article Title:Bound water structure and polymorphic amino acids act together to allow the binding of different peptides to MHC class I HLA-B53.
Reference Detail
Reference ID:1002939
Abstract:The structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 angstrom resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 angstrom) shift in the position of the alpha 1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes.
Date:1996
Reference Type:Literature
PubMed ID:8624812
Journal:Immunity
Journal Volume:4
Article Pages:215-28
Journal ISSN:1074-7613
Article Chemical List:Amino Acids;HLA Antigens;HLA-B53 antigen;Peptides;Water
Article MeSH List:Amino Acid Sequence; Amino Acids(chemistry); Base Sequence; Crystallography, X-Ray; HLA Antigens(chemistry); Humans; Models, Molecular; Molecular Sequence Data; Peptides(chemistry); Polymorphism, Genetic(immunology); Protein Binding(immunology); Protein Conformation; Structure-Activity Relationship; Water(chemistry)
Curation Last Updated:2014-10-03 20:22:18