Crystal structure of staphylococcal enterotoxin B, a superantigen

The three-dimensional structure of staphylococcal enterotoxin B, which is both a toxin and a super-antigen, has been determined to a resolution of 2.5 Å. The unusual main-chain fold containing two domains may represent a general motif adopted by all staphylococcal enterotoxins. The T-cell receptor b...

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Veröffentlicht in:	Nature (London) 1992-10, Vol.359 (6398), p.801-806
Hauptverfasser:	Swaminathan, S., Furey, William, Pletcher, James, Sax, Martin
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Antigenic determinants, haptens, artificial antigens Antigens Antigens, Bacterial - chemistry Antigens, Bacterial - metabolism Binding Sites Biological and medical sciences Cellular biology crystal structure enterotoxin B Enterotoxins - chemistry Enterotoxins - metabolism Fundamental and applied biological sciences. Psychology Fundamental immunology Humanities and Social Sciences Models, Molecular Molecular immunology multidisciplinary Poisons Protein Conformation Protein Structure, Secondary Receptors, Antigen, T-Cell - metabolism Science Science (multidisciplinary) Staphylococcus aureus Toxins X-Ray Diffraction
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Beschreibung
Zusammenfassung:	The three-dimensional structure of staphylococcal enterotoxin B, which is both a toxin and a super-antigen, has been determined to a resolution of 2.5 Å. The unusual main-chain fold containing two domains may represent a general motif adopted by all staphylococcal enterotoxins. The T-cell receptor binding site encompasses a shallow cavity formed by both domains. The MHCII molecule binds to an adjacent site. Another cavity with possible biological activity was also identified.
ISSN:	0028-0836 1476-4687
DOI:	10.1038/359801a0