Toxic Shock Syndrome Toxin-1 Complexed with a Class II Major Histocompatibility Molecule HLA-DR1
| Autor: | Jongsun Kim, Don C. Wiley, Robert G. Urban, Jack L. Strominger |
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| Rok vydání: | 1994 |
| Předmět: |
Models
Molecular musculoskeletal diseases Staphylococcus aureus endocrine system Protein Conformation Stereochemistry T cell Bacterial Toxins Receptors Antigen T-Cell chemical and pharmacologic phenomena Peptide binding Peptide Enterotoxin Biology Crystallography X-Ray Protein Structure Secondary Enterotoxins Antigen Superantigen medicine Humans Binding site chemistry.chemical_classification Binding Sites Superantigens Multidisciplinary T-cell receptor HLA-DR1 Antigen Hydrogen Bonding hemic and immune systems Molecular biology biological factors medicine.anatomical_structure chemistry |
| Zdroj: | Science. 266:1870-1874 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.7997880 |
| Popis: | The three-dimensional structure of a Staphylococcus aureus superantigen, toxic shock syndrome toxin-1 (TSST-1), complexed with a human class II major histocompatibility molecule (DR1), was determined by x-ray crystallography. The TSST-1 binding site on DR1 overlaps that of the superantigen S. aureus enterotoxin B (SEB), but the two binding modes differ. Whereas SEB binds primarily off one edge of the peptide binding site of DR1, TSST-1 extends over almost one-half of the binding site and contacts both the flanking alpha helices of the histocompatibility antigen and the bound peptide. This difference suggests that the T cell receptor (TCR) would bind to TSST-1:DR1 very differently than to DR1:peptide or SEB:DR1. It also suggests that TSST-1 binding may be dependent on the peptide, though less so than TCR binding, providing a possible explanation for the inability of TSST-1 to competitively block SEB binding to all DR1 molecules on cells (even though the binding sites of TSST-1 and SEB on DR1 overlap almost completely) and suggesting the possibility that T cell activation by superantigen could be directed by peptide antigen. |
| Databáze: | OpenAIRE |
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