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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Binding Sites
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Crystallography, X-Ray
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HLA-DR1 Antigen / chemistry*
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HLA-DR1 Antigen / metabolism
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Hemagglutinin Glycoproteins, Influenza Virus
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Hemagglutinins / chemistry*
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Hemagglutinins, Viral / chemistry*
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Humans
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Hydrogen Bonding
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Protein Binding
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Protein Conformation
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Receptors, Antigen, T-Cell / metabolism
Substances
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HLA-DR1 Antigen
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Hemagglutinin Glycoproteins, Influenza Virus
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Hemagglutinins
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Hemagglutinins, Viral
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Peptide Fragments
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Receptors, Antigen, T-Cell
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influenza hemagglutinin (306-318)