The role of a conserved lysine in chloride- and voltage-dependent ClC-0 fast gating.
J Gen Physiol
; 130(4): 351-63, 2007 Oct.
Article
en En
| MEDLINE
| ID: mdl-17846165
ABSTRACT
ClC-0 is a chloride channel whose gating is sensitive to voltage, chloride, and pH. In a previous publication, we showed that the K149C mutation causes a +70-mV shift in the voltage dependence of ClC-0 fast gating. In this paper we analyze the effects of a series of mutations at K149 on the voltage and chloride dependence of gating. By fitting our data to the previously proposed four-state model for ClC-0 fast gating, we show which steps in fast-gate opening are likely to be affected by these mutations. Computational analysis of mutant ClC-0 homology models show electrostatic contributions to chloride binding that may partially account for the effects of K149 on gating. The analysis of gating kinetics in combination with the available structural information suggests some of the structural changes likely to underpin fast-gate opening.
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Activación del Canal Iónico
/
Canales de Cloruro
/
Sustitución de Aminoácidos
/
Lisina
/
Modelos Biológicos
Tipo de estudio:
Diagnostic_studies
/
Prognostic_studies
Límite:
Animals
Idioma:
En
Revista:
J Gen Physiol
Año:
2007
Tipo del documento:
Article
País de afiliación:
Estados Unidos