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Nature. 1994 Apr 21;368(6473):711-8.

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

Author information

1
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.

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.

PMID:
8152483
DOI:
10.1038/368711a0
[Indexed for MEDLINE]

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