Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1.
Nature
; 367(6458): 94-7, 1994 Jan 06.
Article
em En
| MEDLINE
| ID: mdl-8107781
ABSTRACT
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.
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Base de dados:
MEDLINE
Assunto principal:
Toxinas Bacterianas
/
Superantígenos
/
Enterotoxinas
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article