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Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen

Naturevolume 368, pages711–718 (1994)Cite this article

Abstract

The structure of a bacterial superantigen,Staphylococcus aureus enterotoxin B, bound to a human class II histocompatibility complex molecule (HLA-DR1) has been determined by X-ray crystallography. The superantigen binds as an intact protein outside the conventional peptide antigen-binding site of the class II major histocompatibility complex (MHC) molecule. No large conformational changes occur upon complex formation in either the DR1 or the enterotoxin B molecules. The structure of the complex helps explain how different class II molecules and superantigens associate and suggests a model for ternary complex formation with the T-cell antigen receptor (TCR), in which unconventional TCR-MHC contacts are possible.

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Author information

Authors and Affiliations

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

    Theodore S. Jardetzky, Robert G. Urban & Jack L. Strominger

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

    Jerry H. Brown, Lawrence J. Stern & Don C. Wiley

  3. Rosenstiel Research Center, Brandeis University, 415 South Street, Waltham, Massachusetts, 02154, USA

    Jerry H. Brown

  4. Department of Pediatrics, Children's Hospital of Pittsburgh, 6130 Rangos Research Building, 3705 Fifth Avenue, Pittsburgh, Pennsylvania, 15213, USA

    Joan C. Gorga

  5. Department of Biology, Purdue University, West Lafayette, Indiana, 47907, USA

    Young-in Chi & Cynthia Stauffacher

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  1. Theodore S. Jardetzky

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  8. Jack L. Strominger

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Jardetzky, T., Brown, J., Gorga, J.et al. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen.Nature368, 711–718 (1994). https://doi.org/10.1038/368711a0

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