@article{APS4023,
author = {Jing Yao and Hui Li and Ge-liang Gan and Ying Wu and Jiu-ping Ding},
title = {Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca 2+ -activated K + (mSlo1) channels},
journal = {Acta Pharmacologica Sinica},
volume = {27},
number = {7},
year = {2016},
keywords = {},
abstract = {Aim: To gain insight into the interaction between the Charybdotoxin (ChTX) and BK channels.
Methods: Site-directed mutagenesis was used to make two mutants: mSlo1-F266L and mSlo1-F266A. The two mutants were then expressed in Xenopus oocytes and their effects were tested on ChTX by electrophysiology experiments.
Results: We demonstrate an equilibrium dissociation constant Kd= 3.1-4.2 nmol/L for both the mutants mSlo 1-F266L and mSlo 1-F266 A similar to that of the wild-type mSlo1 Kd=3.9 nmol/L.
Conclusion: The residue Phe266 does not play a crucial role in binding to ChTX, which is opposed to the result arising from the simulation of peptide-channel interaction.},
issn = {1745-7254}, url = {http://www.chinaphar.com/article/view/4023}
}