1SEB

COMPLEX OF THE HUMAN MHC CLASS II GLYCOPROTEIN HLA-DR1 AND THE BACTERIAL SUPERANTIGEN SEB

Summary for 1SEB

• Entry DOI: 10.2210/pdb1seb/pdb
• Descriptor: HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, ENDOGENOUS PEPTIDE MODEL, POLY-ALA, ENTEROTOXIN TYPE B, ... (4 entities in total)
• Functional Keywords: histocompatibility antigen, mhc ii, superantigen, enterotoxin peptide, toxin, complex (mhc ii-peptide-toxin) complex, complex (mhc ii/peptide/toxin)
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Single-pass type I membrane protein: P01903 P04229; Secreted: P01552
• Total number of polymer chains: 8
• Total formula weight: 144654.90

Authors

Jardetzky, T.S.,Brown, J.H.,Gorga, J.C.,Stern, L.J.,Urban, R.G.,Chi, Y.I.,Stauffacher, C.,Strominger, J.L.,Wiley, D.C. (deposition date: 1995-11-26, release date: 1996-06-20, Last modification date: 2024-11-06)

Primary citation

Jardetzky, T.S.,Brown, J.H.,Gorga, J.C.,Stern, L.J.,Urban, R.G.,Chi, Y.I.,Stauffacher, C.,Strominger, J.L.,Wiley, D.C.
Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen.
Nature, 368:711-718, 1994

PubMed Abstract: 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.

PubMed: 8152483
DOI: 10.1038/368711a0

Experimental method

X-RAY DIFFRACTION (2.7 Å)