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.
journal_name
Celljournal_title
Cellauthors
Madden DR,Gorga JC,Strominger JL,Wiley DCdoi
10.1016/0092-8674(92)90252-8subject
Has Abstractpub_date
1992-09-18 00:00:00pages
1035-48issue
6eissn
0092-8674issn
1097-4172pii
0092-8674(92)90252-8journal_volume
70pub_type
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