The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHC
作者： Dean R. Madden , Joan C. Gorga , Jack L. Strominger , Don C. Wiley
DOI: 10.1016/0092-8674(92)90252-8
关键词:
摘要: 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 human molecule HLA-B27 provides a detailed composite image co-crystallized collection HLA-B27-bound peptides, indicating that they share common main-chain length. It also permits direct visualization conservation arginine an "anchor" side chain at second position, which is in potentially HLA-B27-specific pocket may therefore have role association with several diseases. Tight binding to appears result from extensive contacts found ends cleft between atoms conserved chains, involve stabilizing three-dimensional fold HLA-B27. concentration interactions termini sequence (and probably some length) variability center peptide, where it exposed for T cell recognition.
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