2I2R

Crystal structure of the KChIP1/Kv4.3 T1 complex

2I2R の概要

• エントリーDOI: 10.2210/pdb2i2r/pdb
• 分子名称: Potassium voltage-gated channel subfamily D member 3, Kv channel-interacting protein 1, ZINC ION, ... (5 entities in total)
• 機能のキーワード: ef-hand protein, complex, potassium channel, ncs protein, calcium binding protein, transport protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: Q62897; Cell membrane; Peripheral membrane protein (By similarity): Q9NZI2
• タンパク質・核酸の鎖数: 16
• 化学式量合計: 303949.37

構造登録者

Findeisen, F.,Pioletti, M.,Minor Jr., D.L. (登録日: 2006-08-16, 公開日: 2006-10-24, 最終更新日: 2023-08-30)

主引用文献

Pioletti, M.,Findeisen, F.,Hura, G.L.,Minor Jr., D.L.
Three-dimensional structure of the KChIP1-Kv4.3 T1 complex reveals a cross-shaped octamer
Nat.Struct.Mol.Biol., 13:987-995, 2006

PubMed Abstract: Brain I(A) and cardiac I(to) currents arise from complexes containing Kv4 voltage-gated potassium channels and cytoplasmic calcium-sensor proteins (KChIPs). Here, we present X-ray crystallographic and small-angle X-ray scattering data that show that the KChIP1-Kv4.3 N-terminal cytoplasmic domain complex is a cross-shaped octamer bearing two principal interaction sites. Site 1 comprises interactions between a unique Kv4 channel N-terminal hydrophobic segment and a hydrophobic pocket formed by displacement of the KChIP H10 helix. Site 2 comprises interactions between a T1 assembly domain loop and the KChIP H2 helix. Functional and biochemical studies indicate that site 1 influences channel trafficking, whereas site 2 affects channel gating, and that calcium binding is intimately linked to KChIP folding and complex formation. Together, the data resolve how Kv4 channels and KChIPs interact and provide a framework for understanding how KChIPs modulate Kv4 function.

PubMed: 17057713
DOI: 10.1038/nsmb1164

実験手法

X-RAY DIFFRACTION (3.35 Å)