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Elucidation of the Covalent and Tertiary Structures of Biologically Active Ts3 Toxin.
- Source :
- Angewandte Chemie International Edition; 7/18/2016, Vol. 55 Issue 30, p8639-8642, 4p
- Publication Year :
- 2016
-
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 (Na<subscript>v</subscript>) 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. [ABSTRACT FROM AUTHOR]
- Subjects :
- VENOM
SODIUM channels
RACEMIC mixtures
RACEMIZATION
PROTEIN structure
Subjects
Details
- Language :
- English
- ISSN :
- 14337851
- Volume :
- 55
- Issue :
- 30
- Database :
- Complementary Index
- Journal :
- Angewandte Chemie International Edition
- Publication Type :
- Academic Journal
- Accession number :
- 116790839
- Full Text :
- https://doi.org/10.1002/anie.201603420