Structural analysis of the S4-S5 linker of the human KCNQ1 potassium channel.
Biochem Biophys Res Commun
; 456(1): 410-4, 2015 Jan 02.
Article
em En
| MEDLINE
| ID: mdl-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.
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Base de dados:
MEDLINE
Assunto principal:
Canal de Potássio KCNQ1
Limite:
Humans
Idioma:
En
Ano de publicação:
2015
Tipo de documento:
Article