Structural highlights
Publication Abstract from PubMed
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.
Residues defining V beta specificity in staphylococcal enterotoxins.,Swaminathan S, Furey W, Pletcher J, Sax M Nat Struct Biol. 1995 Aug;2(8):680-6. PMID:7552730[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Swaminathan S, Furey W, Pletcher J, Sax M. Residues defining V beta specificity in staphylococcal enterotoxins. Nat Struct Biol. 1995 Aug;2(8):680-6. PMID:7552730
