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Product Summary
Fragment
N-terminal domain<br/>Residues 6-145
Protein Description
Potassium channel Kv4.3 complexed with regulatory subunit KChIP1
Background
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.
Protein Classification
membrane protein
Structure Weight
75748.88 Da
PDBID
2NZ0
Method
X-Ray Diffraction
Resolution
3.2 Å
Ligand Chemical Component
Calcium ion; Zinc ion
Reference
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
cDNALength
540 (KCNIP1) 420 (KCNA3)