5cy0
From Proteopedia
Total Chemical Synthesis, Covalent Structure Verification, and X-ray Structure of Bioactive Ts3 Toxin by Racemic Protein Crystallography
Structural highlights
FunctionSCX3_TITSE Binds voltage-dependently at site-3 of sodium channels (Nav) and inhibits the inactivation of the activated channels, thereby blocking neuronal transmission. This toxin is active against mammals (mice).[1] [2] [3] Publication Abstract from PubMedTs3 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. Elucidation of the Covalent and Tertiary Structures of Biologically Active Ts3 Toxin.,Dang B, Kubota T, Mandal K, Correa AM, Bezanilla F, Kent SB Angew Chem Int Ed Engl. 2016 May 31. doi: 10.1002/anie.201603420. PMID:27244051[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
Categories: Large Structures | Tityus serrulatus | Bezanilla F | Correa AM | Dang B | Kent SB | Kubota T | Mandal K
