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| Article Authors: | L J Stern; J H Brown; T S Jardetzky; J C Gorga; R G Urban; J L Strominger; D C Wiley |
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| Article Title: | Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. |
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| Reference ID: | 315104 |
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| 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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| Affiliations: | Department of Biochemistry and Molecular Biology, Harvard University, Cambridge Massachusetts 62138. |
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| Date: | 1994 |
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| Reference Type: | Literature |
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| PubMed ID: | 8145819 |
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| Journal: | Nature |
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| Journal Volume: | 368 |
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| Article Pages: | 215-21 |
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| Journal ISSN: | 1476-4687 |
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| Article Chemical List: | HLA-DR1 Antigen;Hemagglutinin Glycoproteins, Influenza Virus;Hemagglutinins;Hemagglutinins, Viral;Peptide Fragments;Receptors, Antigen, T-Cell;influenza hemagglutinin (306-318) |
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| Article MeSH List: | Amino Acid Sequence; Binding Sites; Crystallography, X-Ray; HLA-DR1 Antigen(chemistry; metabolism); Hemagglutinin Glycoproteins, Influenza Virus; Hemagglutinins(chemistry); Hemagglutinins, Viral(chemistry); Humans; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Peptide Fragments(chemistry); Protein Binding; Protein Conformation; Receptors, Antigen, T-Cell(metabolism) |
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| Article Comments: | Data originally imported from the Database of Functional Molecular Immunology, FIMM (http://sdmc.lit.org.sg:8080/fimm/) |
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| Curation Last Updated: | 2011-08-23 20:45:22 |
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