2nz0
Crystal structure of potassium channel Kv4.3 in complex with its regulatory subunit KChIP1 (CASP Target)
|
OverviewOverview
KChIPs coassemble with pore-forming Kv4 alpha subunits to form a native, complex in the brain and heart and regulate the expression and gating, properties of Kv4 K(+) channels, but the mechanisms underlying these, processes are unknown. Here we report a co-crystal structure of the, complex of human Kv4.3 N-terminus and KChIP1 at a 3.2-A resolution. The, structure reveals a unique clamping action of the complex, in which a, single KChIP1 molecule, as a monomer, laterally clamps two neighboring, Kv4.3 N-termini in a 4:4 manner, forming an octamer. The proximal, N-terminal peptide of Kv4.3 is sequestered by its binding to an elongated, groove on the surface of KChIP1, which is indispensable for the modulation, of Kv4.3 by KChIP1, and the same KChIP1 molecule binds to an adjacent T1, domain to stabilize the tetrameric Kv4.3 channels. Taken together with, biochemical and functional data, our findings provide a structural basis, for the modulation of Kv4 by KChIPs.
About this StructureAbout this Structure
2NZ0 is a Protein complex structure of sequences from Homo sapiens with CA and ZN as ligands. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis for modulation of Kv4 K+ channels by auxiliary KChIP subunits., Wang H, Yan Y, Liu Q, Huang Y, Shen Y, Chen L, Chen Y, Yang Q, Hao Q, Wang K, Chai J, Nat Neurosci. 2007 Jan;10(1):32-9. Epub 2006 Dec 24. PMID:17187064
Page seeded by OCA on Mon Nov 12 23:04:27 2007