1hsa
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THE THREE-DIMENSIONAL STRUCTURE OF HLA-B27 AT 2.1 ANGSTROMS RESOLUTION SUGGESTS A GENERAL MECHANISM FOR TIGHT PEPTIDE BINDING TO MHC
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142830], Hypoproteinemia, hypercatabolic OMIM:[109700], Spondyloarthropathy, susceptibility to, 1 OMIM:[142830], Stevens-Johnson syndrome, carbamazepine-induced, susceptibility to OMIM:[142830]
About this StructureAbout this Structure
1HSA is a Protein complex structure of sequences from Homo sapiens. The following page contains interesting information on the relation of 1HSA with [Major Histocompatibility Complex]. Full crystallographic information is available from OCA.
ReferenceReference
The three-dimensional structure of HLA-B27 at 2.1 A resolution suggests a general mechanism for tight peptide binding to MHC., Madden DR, Gorga JC, Strominger JL, Wiley DC, Cell. 1992 Sep 18;70(6):1035-48. PMID:1525820
Page seeded by OCA on Mon Nov 12 17:21:52 2007