Crystal structure of the human two-pore domain potassium channel K2P1.
Science
; 335(6067): 432-6, 2012 Jan 27.
Article
em En
| MEDLINE
| ID: mdl-22282804
ABSTRACT
Two-pore domain potassium (K(+)) channels (K2P channels) control the negative resting potential of eukaryotic cells and regulate cell excitability by conducting K(+) ions across the plasma membrane. Here, we present the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1 (TWIK-1). Unlike other K(+) channel structures, K2P1 is dimeric. An extracellular cap domain located above the selectivity filter forms an ion pathway in which K(+) ions flow through side portals. Openings within the transmembrane region expose the pore to the lipid bilayer and are filled with electron density attributable to alkyl chains. An interfacial helix appears structurally poised to affect gating. The structure lays a foundation to further investigate how K2P channels are regulated by diverse stimuli.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Canais de Potássio de Domínios Poros em Tandem
Limite:
Humans
Idioma:
En
Revista:
Science
Ano de publicação:
2012
Tipo de documento:
Article
País de afiliação:
Estados Unidos