Referenced in: none

Automatically associated channels: Kv7.1

Title: Structural analysis of the S4-S5 linker of the human KCNQ1 potassium channel.

Authors: Shovanlal Gayen, Qingxin Li, Congbao Kang

Journal, date & volume: Biochem. Biophys. Res. Commun., 2015 Jan 2 , 456, 410-4

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/25475720

Abstract
KCNQ1 plays important roles in the cardiac action potential and consists of an N-terminal domain, a voltage-sensor domain, a pore domain and a C-terminal domain. KCNQ1 is a voltage-gated potassium channel and its channel activity is regulated by membrane potentials. The linker between transmembrane helices 4 and 5 (S4-S5 linker) is important for transferring the conformational changes from the voltage-sensor domain to the pore domain. In this study, the structure of the S4-S5 linker of KCNQ1 was investigated by solution NMR, circular dichroism and fluorescence spectroscopic studies. The S4-S5 linker adopted a helical structure in detergent micelles. The W248 may interact with the cell membrane.