Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Nat Struct Mol Biol 2006 Nov 01;1311:987-95. doi: 10.1038/nsmb1164.
Show Gene links Show Anatomy links

Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer.

Pioletti M , Findeisen F , Hura GL , Minor DL .

Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 voltage-gated potassium channels and cytoplasmic calcium-sensor proteins (KChIPs). Here, we present X-ray crystallographic and small-angle X-ray scattering data that show that the KChIP1-Kv4.3 N-terminal cytoplasmic domain complex is a cross-shaped octamer bearing two principal interaction sites. Site 1 comprises interactions between a unique Kv4 channel N-terminal hydrophobic segment and a hydrophobic pocket formed by displacement of the KChIP H10 helix. Site 2 comprises interactions between a T1 assembly domain loop and the KChIP H2 helix. Functional and biochemical studies indicate that site 1 influences channel trafficking, whereas site 2 affects channel gating, and that calcium binding is intimately linked to KChIP folding and complex formation. Together, the data resolve how Kv4 channels and KChIPs interact and provide a framework for understanding how KChIPs modulate Kv4 function.

PubMed ID: 17057713
PMC ID: PMC3018330
Article link: Nat Struct Mol Biol
Grant support: [+]

Species referenced: Xenopus
Genes referenced: kcnd3 kcnip1

References [+] :
An, Modulation of A-type potassium channels by a family of calcium sensors. 2000, Pubmed, Xenbase