Citation

Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC. 1994. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature. 368(6468):215-221. DOI:10.1038/368215a0

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. Article via http://europepmc.org/abstract/MED/8145819
Nature Publishing Group

Related Faculty

Photo of Jack Strominger

Research Professor and Immunology pioneer Jack Strominger investigates self-tolerance and the immunology of pregnancy. His lab specializes in the structure and function of human histocompatibility proteins and their roles in disease.

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