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

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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Gayen S,Li Q,Kang C

doi

10.1016/j.bbrc.2014.11.097

subject

Has Abstract

pub_date

2015-01-02 00:00:00

pages

410-4

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(14)02138-X

journal_volume

456

pub_type

杂志文章

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