Two N-terminal domains of Kv4 K(+) channels regulate binding to and modulation by KChIP1.
Neuron
; 41(4): 587-98, 2004 Feb 19.
Article
en En
| MEDLINE
| ID: mdl-14980207
ABSTRACT
The family of calcium binding proteins called KChIPs associates with Kv4 family K(+) channels and modulates their biophysical properties. Here, using mutagenesis and X-ray crystallography, we explore the interaction between Kv4 subunits and KChIP1. Two regions in the Kv4.2 N terminus, residues 7-11 and 71-90, are necessary for KChIP1 modulation and interaction with Kv4.2. When inserted into the Kv1.2 N terminus, residues 71-90 of Kv4.2 are also sufficient to confer association with KChIP1. To provide a structural framework for these data, we solved the crystal structures of Kv4.3N and KChIP1 individually. Taken together with the mutagenesis data, the individual structures suggest that that the Kv4 N terminus is required for stable association with KChIP1, perhaps through a hydrophobic surface interaction, and that residues 71-90 in Kv4 subunits form a contact loop that mediates the specific association of KChIPs with Kv4 subunits.
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Base de datos:
MEDLINE
Asunto principal:
Proteínas de Unión al Calcio
/
Canales de Potasio
/
Membrana Celular
/
Canales de Potasio con Entrada de Voltaje
Idioma:
En
Revista:
Neuron
Asunto de la revista:
NEUROLOGIA
Año:
2004
Tipo del documento:
Article