2NZ0

Crystal structure of potassium channel Kv4.3 in complex with its regulatory subunit KChIP1

Summary for 2NZ0

• Entry DOI: 10.2210/pdb2nz0/pdb
• Descriptor: Kv channel-interacting protein 1, Potassium voltage-gated channel subfamily D member 3, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: kv4.3, kchip1, membrane protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Peripheral membrane protein (By similarity): Q9NZI2; Membrane; Multi-pass membrane protein: Q9UK17
• Total number of polymer chains: 4
• Total formula weight: 75748.37

Authors

Wang, H.,Yan, Y.,Shen, Y.,Chen, L.,Wang, K. (deposition date: 2006-11-22, release date: 2006-12-26, Last modification date: 2023-12-27)

Primary citation

Wang, H.,Yan, Y.,Liu, Q.,Huang, Y.,Shen, Y.,Chen, L.,Chen, Y.,Yang, Q.,Hao, Q.,Wang, K.,Chai, J.
Structural basis for modulation of Kv4 K(+) channels by auxiliary KChIP subunits.
Nat.Neurosci., 10:32-39, 2007

PubMed Abstract: 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.

PubMed: 17187064
DOI: 10.1038/nn1822

Experimental method

X-RAY DIFFRACTION (3.2 Å)