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


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-04

AUTHORS

T S Jardetzky, J H Brown, J C Gorga, L J Stern, R G Urban, Y I Chi, C Stauffacher, J L Strominger, D C Wiley

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. More... »

PAGES

711-718

Journal

TITLE

Nature

ISSUE

6473

VOLUME

368

Author Affiliations

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/368711a0

DOI

http://dx.doi.org/10.1038/368711a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1021670380

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/8152483


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