Summary
PDB 1SEB deposited: 1995-11-26 modified: 2009-02-24
Title COMPLEX OF THE HUMAN MHC CLASS II GLYCOPROTEIN HLA-DR1 AND THE BACTERIAL SUPERANTIGEN SEB
Authors Brown, J.H., Chi, Y.I., Gorga, J.C., Jardetzky, T.S., Stauffacher, C., Stern, L.J., Strominger, J.L., Urban, R.G., Wiley, D.C.
Method X-RAY DIFFRACTION
Structure factors resolution None rfactor None rfree None
DPI
Citations

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.

Nature. 1994 Apr 21;368(6473):711-8.

Cross References
Database source Identifier Description
PubMed 8152483 NATUAS
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
1SEB/1 1SEB 1 octamer 0 8 0 8798