Structural principles that govern the peptide-binding motifs of class I MHC molecules - PubMed (original) (raw)

. 1998 Sep 4;281(5):929-47.

doi: 10.1006/jmbi.1998.1982.

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Structural principles that govern the peptide-binding motifs of class I MHC molecules

C Zhang et al. J Mol Biol. 1998.

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Abstract

The peptides that bind class I MHC molecules are restricted in length and often contain key amino acids, anchor residues, at particular positions. The side-chains of peptide anchor residues interact with the polymorphic complementary pockets in MHC peptide-binding grooves and provide the molecular basis for allele-specific recognition of antigenic peptides. We establish correlations between class I MHC specificities for anchor residues and class I MHC sequence markers that occur at the polymorphic positions lining the structural pockets. By analyzing the pocket structures of nine crystallized class I MHC molecules and the modeled structures of another 39 class I MHC molecules, we show that class I pockets can be classified into families that are distinguishable by their common physico-chemical properties and peptide side-chain selectivities. The identification of recurrent structural principles among class I pockets makes it possible to greatly expand the repertoire of known peptide-binding motifs of class I MHC molecules. The evolutionary strategies underlying the emergence of pocket families is briefly discussed.

Copyright 1998 Academic Press

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