Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca2+-activated K~+(mSlo1)channels

作     者：Jmg YAO~2 Hui LI~2 Ge-liang GAN Ying WU Jiu-ping DING~3 Institute of Biochemistry and Biophysics,College of Life Science and Technology,Huazhong University of Science and Technology,Wuhan 430074,China 

作者机构：Institute of Biochemistry and Biophysics College of Life Science and Technology Huazhong University of Science and Technology Wuhan China 

出 版 物：《Acta Pharmacologica Sinica》 (中国药理学报(英文版))

年 卷 期：2006年第27卷第7期

页      面：945-949页

核心收录：

学科分类：1007[医学-药学(可授医学、理学学位)] 1006[医学-中西医结合] 100706[医学-药理学] 0703[理学-化学] 100602[医学-中西医结合临床] 10[医学] 

基　　金：Project supported by Grants from the National Natural Science Foundation of China(30470449) 

主　　题：charybdotoxin large-conductance calciumactivated potassium channelss Slo1 

摘      要：Aim:To gain insight into the interaction between the Charybdotoxin(ChTX)andBK ***:Site-directed mutagenesis was used to make two mutants:mSlol-F266L and *** two mutants were then expressed in Xeno-pus oocytes and their effects were tested on ChTX by ***:We demonstrate an equilibrium dissociation constant Kd=3.1—4.2 nmol/L for both the mutants mSlol-F266L and mSlol-F266A similar to thatof the wild-type mSlol Kd=3.9 nmol/***:The residue Phe266 does notplay a crucial role in binding to ChTX,which is opposed to the result arising fromthe simulation of peptide-channel interaction.