Publication Abstract from PubMed
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.
Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide.,Stern LJ, Brown JH, Jardetzky TS, Gorga JC, Urban RG, Strominger JL, Wiley DC Nature. 1994 Mar 17;368(6468):215-21. PMID:8145819[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
