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Nature. 1994 Mar 17;368(6468):215-21.

Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide.

Author information

1
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge Massachusetts 62138.

Abstract

An influenza virus peptide binds to HLA-DR1 in an extended conformation with a pronounced twist. Thirty-five per cent of the peptide surface is accessible to solvent and potentially available for interaction with the antigen receptor on T cells. Pockets in the peptide-binding site accommodate five of the thirteen side chains of the bound peptide, and explain the peptide specificity of HLA-DR1. Twelve hydrogen bonds between conserved HLA-DR1 residues and the main chain of the peptide provide a universal mode of peptide binding, distinct from the strategy used by class I histocompatibility proteins.

PMID:
8145819
DOI:
10.1038/368215a0
[Indexed for MEDLINE]

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