TY - JOUR AU - Yao Jing AU - Li Hui AU - Gan Ge-liang AU - Wu Ying AU - Ding Jiu-ping PY - 2016 TI - Residue Phe266 in S5-S6 loop is not critical for Charybdotoxin binding to Ca 2+ -activated K + (mSlo1) channels JF - Acta Pharmacologica Sinica; Vol 27, No 7 (July 2006): Acta Pharmacologica Sinica(Special Issue on Calcium signaling) Y2 - 2016 KW - N2 - 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 K d= 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 K d=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. UR - http://www.chinaphar.com/article/view/4023