Epitopes described in "The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC."

Reference
Article Authors:D R Madden; J C Gorga; J L Strominger; D C Wiley
Article Title:The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC.
Reference Detail
Reference ID:1013590
Abstract:Cell surface complexes of class I MHC molecules and bound peptide antigens serve as specific recognition elements controlling the cytotoxic immune response. The 2.1 A structure of the human class I MHC molecule HLA-B27 provides a detailed composite image of a co-crystallized collection of HLA-B27-bound peptides, indicating that they share a common main-chain structure and length. It also permits direct visualization of the conservation of arginine as an "anchor" side chain at the second peptide position, which is bound in a potentially HLA-B27-specific pocket and may therefore have a role in the association of HLA-B27 with several diseases. Tight peptide binding to class I MHC molecules appears to result from the extensive contacts found at the ends of the cleft between peptide main-chain atoms and conserved MHC side chains, which also involve the peptide in stabilizing the three-dimensional fold of HLA-B27. The concentration of binding interactions at the peptide termini permits extensive sequence (and probably some length) variability in the center of the peptide, where it is exposed for T cell recognition.
Date:1992
Reference Type:Literature
PubMed ID:1525820
Journal:Cell
Journal Volume:70
Article Pages:1035-48
Journal ISSN:0092-8674
Article Chemical List:HLA-B27 Antigen;Arginine
Article MeSH List:Amino Acid Sequence; Arginine(metabolism); HLA-B27 Antigen(chemistry); Humans; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Structure-Activity Relationship; X-Ray Diffraction
Curation Last Updated:2014-04-01 20:05:46