1. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen.
- Author
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Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, Chi YI, Stauffacher C, Strominger JL, and Wiley DC
- Subjects
- Amino Acid Sequence, Animals, Crystallography, X-Ray, Enterotoxins immunology, Humans, Macromolecular Substances, Mice, Models, Molecular, Molecular Sequence Data, Receptors, Antigen, T-Cell metabolism, Staphylococcus aureus immunology, Superantigens immunology, Enterotoxins chemistry, HLA-DR1 Antigen chemistry, Superantigens chemistry
- 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.
- Published
- 1994
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