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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Jardetzky, T., Brown, J., Gorga, J. et al. Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. Nature 368, 711–718 (1994). https://doi.org/10.1038/368711a0
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DOI: https://doi.org/10.1038/368711a0
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