Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

Superantigens stimulate T cells bearing particular T-cell receptor V beta sequences, so they are extremely potent polyclonal T-cell mitogens. T-cell activation is preceded by binding of superantigens to class II major histocompatibility complex (MHC) molecules. To further the structural characterization of these interactions, the crystal structure of a toxin associated with toxic-shock syndrome, TSST-1, which is a microbial superantigen, has been determined at 2.5 A resolution. The N- and C-terminal domains of the structure both contain regions involved in MHC class II association; the C-terminal domain is also implicated in binding the T-cell receptor. Despite low sequence conservation, the TSST-1 topology is similar to the structure reported for the superantigen staphylococcal enterotoxin B4. But TSST-1 lacks several of the structural features highlighted as central to superantigen activity in the staphylococcal enterotoxin B and we therefore reappraise the structural basis of superantigen action.

Original publication

DOI

10.1038/367094a0

Type

Journal article

Journal

Nature

Publication Date

06/01/1994

Volume

367

Pages

94 - 97

Keywords

Amino Acid Sequence, Bacterial Toxins, Computer Graphics, Crystallography, X-Ray, Enterotoxins, Histocompatibility Antigens Class II, Molecular Sequence Data, Protein Conformation, Protein Structure, Secondary, Receptors, Antigen, T-Cell, alpha-beta, Staphylococcus aureus, Structure-Activity Relationship, Superantigens