RGD Reference Report - Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer. - Rat Genome Database

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

Authors: Pioletti, Marta  Findeisen, Felix  Hura, Greg L  Minor, Daniel L 
Citation: Pioletti M, etal., Nat Struct Mol Biol. 2006 Nov;13(11):987-95. Epub 2006 Oct 22.
RGD ID: 13432266
Pubmed: PMID:17057713   (View Abstract at PubMed)
PMCID: PMC3018330   (View Article at PubMed Central)
DOI: DOI:10.1038/nsmb1164   (Journal Full-text)

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.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
protein binding enablesIPIUniProtKB:Q9NZI213432266PMID:17057713IntAct 

Objects Annotated

Genes (Rattus norvegicus)
Kcnd3  (potassium voltage-gated channel subfamily D member 3)


Additional Information