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Article

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

Acta pharmacologica Sinica - 1 Jul 2006

Yao Jing, Li Hui, Gan Ge-liang, Wu Ying, Ding Jiu-ping

Abstract excerpt

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...

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Identifiers

PMID: 16787581
DOI: 10.1111/j.1745-7254.2006.00385.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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