Residues defining Vβ specificity in staphylococcal enterotoxins
- 1 August 1995
- journal article
- research article
- Published by Springer Nature in Nature Structural & Molecular Biology
- Vol. 2 (8) , 680-686
- https://doi.org/10.1038/nsb0895-680
Abstract
The three-dimensional structure of staphylococcal enterotoxin C2 has been determined at 2.7 Å resolution by X-ray diffraction, while the structures of enterotoxins A and E have been modelled based on their sequence homology to other staphylococcal enterotoxins. The T-cell receptor-binding sites of staphylococcal enterotoxin (SE) B and SEC2 are compared and the stereochemical interactions likely to be responsible for their differing Vβ specificities are identified. A similar comparison is made between SEA and SEE.Keywords
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