Catalog # or name ...
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.
Kv channel-interacting protein 1
180 amino acids
Potassium voltage-gated channel subfamily D member 3
140 amino acids
Ligand Chemical Component
Calcium ion; Zinc ion
KCHIP1; MGC95; VABP; A-type potassium channel modulatory protein 1; potassium channel interacting protein 1; vesicle APC-binding protein; Kv channel interacting protein 1
calcium ion binding; potassium channel activity; potassium ion binding; protein binding; voltage-gated ion channel activity
HGK5;HLK3; HPCN3; HUKIII; KV1.3; MK3; PCN3; OTTHUMP00000032397; potassium channel 3; type n potassium channel; voltage-gated potassium channel protein Kv1.3
delayed rectifier potassium channel activity; potassium ion binding; protein binding
Wang, H., Yan, Y., Liu, Q., Huang, Y., Shen, Y., Chen, L., Chen, Y., Yang, Q., Hao, Q., Wang, K., Chai, J. (2007) Structural basis for modulation of Kv4 K(+) channels by auxiliary KChIP subunits. Nat.Neurosci. 10: 32-39
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