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

LJ Stern, JH Brown, TS Jardetzky, JC Gorga, RG Urban… - Nature, 1994 - nature.com
LJ Stern, JH Brown, TS Jardetzky, JC Gorga, RG Urban, JL Strominger, DC Wiley
Nature, 1994nature.com
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 …
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.
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