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

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

Author information

1
Department of Biomedical Engineering, Boston University College of Engineering, Boston, MA, 02215, USA.

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.

PMID:
9719645
DOI:
10.1006/jmbi.1998.1982
[Indexed for MEDLINE]

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