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Kv4.3 with KChIP1 Protein Crystal

(CBCRY08)  Download Datasheet
Background
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 Da
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 Å
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 ID
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
Gene ID
3738
Chromosome Location
1p13.3
Function
delayed rectifier potassium channel activity; potassium ion binding; protein binding
Reference
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