Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen.
The structure of a bacterial superantigen, Staphylococcus aureus enterotoxin B, bound to a human class II histocompatibility complex molecule (HLA-DR1) has been determined by X-ray crystallography. The superantigen binds as an intact protein outside the conventional peptide antigen-binding site of the class II major histocompatibility complex (MHC) molecule. No large conformational changes occur upon complex formation in either the DR1 or the enterotoxin B molecules. The structure of the complex helps explain how different class II molecules and superantigens associate and suggests a model for ternary complex formation with the T-cell antigen receptor (TCR), in which unconventional TCR-MHC contacts are possible.
Jardetzky
T S
TS
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
Brown
J H
JH
Gorga
J C
JC
Stern
L J
LJ
Urban
R G
RG
Chi
Y I
YI
Stauffacher
C
C
Strominger
J L
JL
Wiley
D C
DC
D000595:Amino Acid Sequence; D000818:Animals; D018360:Crystallography, X-Ray; D004768:Enterotoxins / Q000737:chemistry* / Q000276:immunology; D015798:HLA-DR1 Antigen / Q000737:chemistry*; D006801:Humans; D046911:Macromolecular Substances; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011948:Receptors, Antigen, T-Cell / Q000378:metabolism; D013211:Staphylococcus aureus / Q000276:immunology; D018089:Superantigens / Q000737:chemistry* / Q000276:immunology
D004768:Enterotoxins; D015798:HLA-DR1 Antigen; D046911:Macromolecular Substances; D011948:Receptors, Antigen, T-Cell; D018089:Superantigens; C031818:enterotoxin B, staphylococcal