Epitopes described in "The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain."

Reference
Article Authors:E J Collins; D N Garboczi; M N Karpusas; D C Wiley
Article Title:The three-dimensional structure of a class I major histocompatibility complex molecule missing the alpha 3 domain of the heavy chain.
Reference Detail
Reference ID:1013620
Abstract:Class I major histocompatibility complex (MHC) molecules are ternary complexes of the soluble serum protein beta 2-microglobulin, MHC heavy chain, and bound peptide. The first two domains (alpha 1, alpha 2) of the heavy chain create the peptide binding cleft and the surface that contacts the T-cell receptor. The third domain (alpha 3) associates with the T-cell co-receptor, CD8, during T-cell recognition. Here we describe the x-ray crystal structure of a human class I MHC molecule, HLA-Aw68, from which the alpha 3 domain has been proteolytically removed. The resulting molecule shows no gross morphological changes compared to the intact protein. A decameric peptide complexed with the intact HLA-Aw68 is seen to bind to the proteolized molecule in the conventional manner, demonstrating that the alpha 3 domain is not required for the structural integrity of the molecule or for peptide binding.
Date:1995
Reference Type:Literature
PubMed ID:7862664
Journal:Proc Natl Acad Sci U S A
Journal Volume:92
Article Pages:1218-21
Journal ISSN:1091-6490
Article Chemical List:HLA-A Antigens;HLA-A*68 antigen;Peptide Fragments
Article MeSH List:Amino Acid Sequence; Cell Line; Crystallography, X-Ray; HLA-A Antigens(chemistry; metabolism); Humans; Hydrolysis; Molecular Sequence Data; Peptide Fragments(chemistry; metabolism); Protein Binding; Protein Structure, Tertiary
Curation Last Updated:2014-10-03 21:19:59