Block of ShakerB K+ channels by Pil, a novel class of scorpion toxin

被引：22

作者：

GomezLagunas, F ^{[1
]}

OlamendiPortugal, T ^{[1
]}

Possani, LD ^{[1
]}

机构：

[1] UNIV NACL AUTONOMA MEXICO,INST BIOTECHNOL,DEPT MOL RECOGNIT & STRUCT BIOL,CUERNAVACA 62271,MORELOS,MEXICO

来源：

FEBS LETTERS | 1997年 / 400卷 / 02期

关键词：

ShakerB; Pandinus; Pil; potassium channel; scorpion toxin;

D O I：

10.1016/S0014-5793(96)01387-7

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Here we describe the basic features of the interaction of K+ channels with Pi1, a recently described 35 amino acid scorpion toxin, which has four disulfide bridges instead of the three commonly found in all the other known scorpion toxins, We found that: (a) Pi1 blocks ShakerB from the outside with a 1:1 stoichiometry, and a K-d of 32 nM in zero external [K+]; (b) extracellular K+, Rb+ and Cs+ but not NH4+ ions strongly impede (destabilize) the block by this toxin; interestingly (c) the destabilizing binding of K+, Rb+, and Cs+ is described by a Hill coefficient n > 1; (d) external K+ is more effective than internal K+ to reduce the block by Pi1.

引用

页码：197 / 200

页数：4

共 12 条

[1] INTERACTION OF TETRAETHYLAMMONIUM ION DERIVATIVES WITH POTASSIUM CHANNELS OF GIANT AXONS [J].