Crystal structure of staphylococcal enterotoxin B, a superantigen.
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.
Swaminathan
S
S
Biocrystallography Laboratory, VA Medical Center, Pittsburgh, Pennsylvania 15240.
Furey
W
W
Pletcher
J
J
Sax
M
M
D000818:Animals; D000942:Antigens, Bacterial / Q000737:chemistry / Q000378:metabolism; D001665:Binding Sites; D004768:Enterotoxins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism; D013211:Staphylococcus aureus; D014961:X-Ray Diffraction
D000942:Antigens, Bacterial; D004768:Enterotoxins; D011948:Receptors, Antigen, T-Cell; C031818:enterotoxin B, staphylococcal