5CY0
Total Chemical Synthesis, Covalent Structure Verification, and X-ray Structure of Bioactive Ts3 Toxin by Racemic Protein Crystallography
Summary for 5CY0
| Entry DOI | 10.2210/pdb5cy0/pdb |
| Descriptor | Ts3 Toxin, GLYCEROL (3 entities in total) |
| Functional Keywords | racemic structure, nav ligand, central symmetric, toxin |
| Biological source | Tityus serrulatus (Brazilian scorpion) |
| Total number of polymer chains | 1 |
| Total formula weight | 7741.72 |
| Authors | Dang, B.,Kubota, T.,Mandal, K.,Correa, A.M.,Bezanilla, F.,Kent, S.B. (deposition date: 2015-07-29, release date: 2016-06-01, Last modification date: 2024-11-20) |
| Primary citation | Dang, B.,Kubota, T.,Mandal, K.,Correa, A.M.,Bezanilla, F.,Kent, S.B. Elucidation of the Covalent and Tertiary Structures of Biologically Active Ts3 Toxin. Angew.Chem.Int.Ed.Engl., 55:8639-8642, 2016 Cited by PubMed Abstract: Ts3 is an alpha scorpion toxin from the venom of the Brazilian scorpion Tityus serrulatus. Ts3 binds to the domain IV voltage sensor of voltage-gated sodium channels (Nav ) and slows down their fast inactivation. The covalent structure of the Ts3 toxin is uncertain, and the structure of the folded protein molecule is unknown. Herein, we report the total chemical synthesis of four candidate Ts3 toxin protein molecules and the results of structure-activity studies that enabled us to establish the covalent structure of biologically active Ts3 toxin. We also report the synthesis of the mirror image form of the Ts3 protein molecule, and the use of racemic protein crystallography to determine the folded (tertiary) structure of biologically active Ts3 toxin by X-ray diffraction. PubMed: 27244051DOI: 10.1002/anie.201603420 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.93 Å) |
Structure validation
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