Potassium channel Kv4.3 with regulatory subunit KChIP1

Cat. No.

CBCRY08

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.

Molecular description

Protein Classification

membrane protein

Structure Weight

75748.88

Polymer

1

Molecule

Kv channel-interacting protein 1

Chain Length

180 amino acids

Polymer

2

Molecule

Potassium voltage-gated channel subfamily D member 3 

Chain Length

140 amino acids

Crystal Description

PDB ID

2NZ0

MMDB ID

43547

Source

E.coli

Method

X-Ray Diffraction

Resolution

3.2 ?

Ligand Chemical Component

Calcium ion; Zinc ion

Gene information

Gene Name

KCNIP1

Synonyms

KCHIP1; MGC95; VABP; A-type potassium channel modulatory protein 1; potassium channel interacting protein 1; vesicle APC-binding protein; Kv channel interacting protein 1

UniProt ID

Q9NZI2

Gene Name

30820

Chromosome  Location

5q35.1

Function

calcium ion binding; potassium channel activity; potassium ion binding; protein binding; voltage-gated ion channel activity

Gene Name

KCNA3

Synonyms

HGK5;HLK3; HPCN3; HUKIII; KV1.3; MK3; PCN3; OTTHUMP00000032397; potassium channel 3; type n potassium channel; voltage-gated potassium channel protein Kv1.3

UniProt ID

P22001

GeneID

3738

Chromosome  Location

1p13.3

Function

delayed rectifier potassium channel activity; potassium ion binding; protein binding

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