Disulfide bridges and blockage of Shaker BK+-channels by another butantoxin peptide purified from the Argentinean scorpion Tityus trivittatus

被引：26

作者：

Coronas, FV

de Roodt, AR

Olamendi-Portugal, T

Zamudio, FZ

Batista, CVF

Gómez-Lagunas, F

Possani, LD

机构：

[1] Univ Nacl Autonoma Mexico, Inst Biotechnol, Dept Mol Recognit & Struct Biol, Cuernavaca 62210, Morelos, Mexico

[2] Adm Nacl Labs, Natl Inst Prod Biol, Buenos Aires, DF, Argentina

[3] Inst Salud Dr Carlos G Malbran, Buenos Aires, DF, Argentina

[4] Univ Nacl Autonoma Mexico, Sch Med, Dept Physiol, Mexico City 04510, DF, Mexico

来源：

TOXICON | 2003年 / 41卷 / 02期

关键词：

butantoxin; disulfide bridge; K+-channel; scorpion toxin; Shaker B;

D O I：

10.1016/S0041-0101(02)00247-7

中图分类号：

R9 [药学];

学科分类号：

1007 ;

摘要：

A peptide was isolated from the venom of the scorpion Tityus trivittatus. It is an isoform of the toxin TsTX-IV earlier described [Toxicon 37 (1999) 651] and identical to butantoxin [Arch. Biochem. Biophys. 379 (2000) 18], both isolated from the Brazilian scorpion Tityus serrulatus. This newly characterized peptide contains 40 amino acid residues with a molecular mass of [M + H+] 4507.0, cross-linked by four disulfide bridges, made between the cysteine pairs: Cys2-Cys5, Cys10-Cys31, Cys16-Cys36 and Cys20-Cys38. It blocks in a completely reversible manner the Shaker B K+-channels, with a K-d around 660 nM. It belongs to the sub-family 12 and it is now being classified as alpha-KTx 12.2. (C) 2002 Elsevier Science Ltd. All rights reserved.

引用

页码：173 / 179

页数：7

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