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Three-dimensional structure of a human class II histocompatibility molecule complexed with superantigen.
- Source :
-
Nature [Nature] 1994 Apr 21; Vol. 368 (6473), pp. 711-8. - Publication Year :
- 1994
-
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.
- Subjects :
- Amino Acid Sequence
Animals
Crystallography, X-Ray
Enterotoxins immunology
Humans
Macromolecular Substances
Mice
Models, Molecular
Molecular Sequence Data
Receptors, Antigen, T-Cell metabolism
Staphylococcus aureus immunology
Superantigens immunology
Enterotoxins chemistry
HLA-DR1 Antigen chemistry
Superantigens chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 0028-0836
- Volume :
- 368
- Issue :
- 6473
- Database :
- MEDLINE
- Journal :
- Nature
- Publication Type :
- Academic Journal
- Accession number :
- 8152483
- Full Text :
- https://doi.org/10.1038/368711a0