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Residues defining V beta specificity in staphylococcal enterotoxins
S Swaminathan1, W Furey, J Pletcher
1Biocrystallography Laboratory, VA Medical Center, Pittsburgh, Pennsylvania 15240, USA.
Nature Structural Biology
|August 1, 1995
Abstract:
The three-dimensional structure of staphylococcal enterotoxin C2 has been determined at 2.7 A 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 V beta specificities are identified. A similar comparison is made between SEA and SEE.