Abstract
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.
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Swaminathan, S., Furey, W., Pletcher, J. et al. Crystal structure of staphylococcal enterotoxin B, a superantigen. Nature 359, 801–806 (1992). https://doi.org/10.1038/359801a0
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DOI: https://doi.org/10.1038/359801a0
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