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

Nature volume 368, pages 215–221 (1994)Cite this article

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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Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    Robert G. Urban & Jack L. Strominger

  2. Howard Hughes Medical Institute, Harvard University, 7 Divinity Avenue, Cambridge, Massachusetts, 02138, USA

    Lawrence J. Stern, Theodore S. Jardetzky & Don C. Wiley

  3. Rosenstiel Research Center, Brandeis University, 415 South Street, Waltham, Massachusetts, 02254, USA

    Jerry H. Brown

  4. Rangos Research Center, Children's Hospital of Pittsburgh and University of Pittsburgh Medical Center, 3705 Fifth Avenue, Pittsburgh, Pennsylvania, 15213, USA

    Joan C. Gorga

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  1. Lawrence J. Stern
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Stern, L., Brown, J., Jardetzky, T. et al. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide. Nature 368, 215–221 (1994). https://doi.org/10.1038/368215a0

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