Bound Water Structure and Polymorphic Amino Acids Act Together to Allow the Binding of Different Peptides to MHC Class I HLA-B53
1996; Cell Press; Volume: 4; Issue: 3 Linguagem: Inglês
10.1016/s1074-7613(00)80430-6
ISSN1097-4180
AutoresKathrine J. Smith, Scott W. Reid, Karl Harlos, Andrew J. McMichael, David I. Stuart, John I. Bell, E. Yvonne Jones,
Tópico(s)T-cell and B-cell Immunology
ResumoThe structure of the human MHC class I molecule HLA-B53 complexed to two nonameric peptide epitopes (from the malaria parasite P. falciparum and the HIV2 gag protein) has been determined by X-ray crystallography at 2.3 Å resolution. The structures reveal the architecture of a Pro-specific B pocket common to many HLA-B alleles. Relative to other alleles, the B53 peptide-binding groove is widened by a significant (up to 1.25 Å) shift in the position of the α1 helix. Within this groove, bound water molecules, acting in concert with the side chains of polymorphic residues, provide the functional malleability of the MHC, which enables the high affinity/low specificity binding of multiple peptide epitopes.
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