The Refined Crystal Structure of Toxic Shock Syndrome Toxin-1 at 2.07 Å Resolution
| Autor: | K. R. Acharya, Rossalyn D. Brehm, Demetres D. Leonidas, Anastassios C. Papageorgiou, Howard S. Tranter |
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| Rok vydání: | 1996 |
| Předmět: |
Models
Molecular Staphylococcus aureus Protein Conformation Stereochemistry Bacterial Toxins Molecular Sequence Data Receptors Antigen T-Cell Biology Crystallography X-Ray medicine.disease_cause Major histocompatibility complex Enterotoxins Protein structure Antigen Structural Biology medicine Superantigen Amino Acid Sequence Binding site Molecular Biology Binding Sites Superantigens Sequence Homology Amino Acid Toxin T-cell receptor HLA-DR1 Antigen Histocompatibility Antigens Class II Water Toxic shock syndrome medicine.disease biology.protein |
| Zdroj: | Journal of Molecular Biology. 260:553-569 |
| ISSN: | 0022-2836 |
| Popis: | The pyrogenic toxin toxic shock syndrome toxin-1 from Staphylococcus aureus is a causative agent of the toxic shock syndrome disease. It belongs to a family of proteins known as superantigens that cross-link major histocompatibility class II molecules and T-cell receptors leading to the activation of a substantial number of T cells. The crystal structure of this protein has been refined to 2.07 A with an Rcryst value of 20.4% for 51,240 reflections. The final model contains three molecules in the asymmetric unit with good stereochemistry and a root-mean-square deviation of 0.009 A and 1.63 from ideality for bond lengths and bond angles, respectively. The overall fold is considerably similar to that of other known microbial superantigens (staphylococcal enterotoxins). However, a detailed structural analysis shows that toxic shock syndrome toxin-1 lacks several structural features that affect its specificity for V beta elements of the T-cell receptor and also its recognition by major histocompatibility class II molecules. |
| Databáze: | OpenAIRE |
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