Residues defining V beta specificity in staphylococcal enterotoxins.
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.
Swaminathan
S
S
Biocrystallography Laboratory, VA Medical Center, Pittsburgh, Pennsylvania 15240, USA.
Furey
W
W
Pletcher
J
J
Sax
M
M
D000595:Amino Acid Sequence; D001665:Binding Sites; D018360:Crystallography, X-Ray / Q000379:methods; D004768:Enterotoxins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D013211:Staphylococcus aureus
D004768:Enterotoxins; D011948:Receptors, Antigen, T-Cell; C049463:enterotoxin E, Staphylococcal; C026066:enterotoxin A, Staphylococcal; C031818:enterotoxin B, staphylococcal; C034959:enterotoxin C, staphylococcal