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

Abstract

AbstractAim: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… (More)
DOI: 10.1111/j.1745-7254.2006.00385.x

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