
doi: 10.1038/359801a0
pmid: 1436058
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 A. 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.
Models, Molecular, Antigens, Bacterial, Staphylococcus aureus, Binding Sites, Protein Conformation, Receptors, Antigen, T-Cell, Protein Structure, Secondary, Enterotoxins, X-Ray Diffraction, Animals
Models, Molecular, Antigens, Bacterial, Staphylococcus aureus, Binding Sites, Protein Conformation, Receptors, Antigen, T-Cell, Protein Structure, Secondary, Enterotoxins, X-Ray Diffraction, Animals
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