Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen. Nature 1994 Apr 21;368(6473):711-8
Date
04/21/1994Pubmed ID
8152483DOI
10.1038/368711a0Scopus ID
2-s2.0-23444454615 (requires institutional sign-in at Scopus site) 525 CitationsAbstract
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.
Author List
Jardetzky TS, Brown JH, Gorga JC, Stern LJ, Urban RG, Chi YI, Stauffacher C, Strominger JL, Wiley DCAuthor
Young-In Chi PhD Assistant Professor in the Surgery department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
Amino Acid SequenceAnimals
Crystallography, X-Ray
Enterotoxins
HLA-DR1 Antigen
Humans
Macromolecular Substances
Mice
Models, Molecular
Molecular Sequence Data
Receptors, Antigen, T-Cell
Staphylococcus aureus
Superantigens
