1S6C

Crystal structure of the complex between KChIP1 and Kv4.2 N1-30

1S6C の概要

• エントリーDOI: 10.2210/pdb1s6c/pdb
• 関連するPDBエントリー: 1NN7
• 分子名称: Kv4 potassium channel-interacting protein KChIP1b, Potassium voltage-gated channel subfamily D member 2, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: ef-hand, transport protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cell membrane; Peripheral membrane protein (By similarity): Q8R426; Cell membrane; Multi-pass membrane protein: Q63881
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 24807.98

構造登録者

Zhou, W.,Qian, Y.,Kunjilwar, K.,Pfaffinger, P.J.,Choe, S. (登録日: 2004-01-23, 公開日: 2004-02-24, 最終更新日: 2024-11-20)

主引用文献

Zhou, W.,Qian, Y.,Kunjilwar, K.,Pfaffinger, P.J.,Choe, S.
Structural insights into the functional interaction of KChIP1 with Shal-type K(+) channels.
Neuron, 41:573-586, 2004

PubMed Abstract: Four Kv channel-interacting proteins (KChIP1 through KChIP4) interact directly with the N-terminal domain of three Shal-type voltage-gated potassium channels (Kv4.1, Kv4.2, and Kv4.3) to modulate cell surface expression and function of Kv4 channels. Here we report a 2.0 Angstrom crystal structure of the core domain of KChIP1 (KChIP1*) in complex with the N-terminal fragment of Kv4.2 (Kv4.2N30). The complex reveals a clam-shaped dimeric assembly. Four EF-hands from each KChIP1 form each shell of the clam. The N-terminal end of Kv4.2 forming an alpha helix (alpha1) and the C-terminal alpha helix (H10) of KChIP1 are enclosed nearly coaxially by these shells. As a result, the H10 of KChIP1 and alpha1 of Kv4.2 mediate interactions between these two molecules, structurally reminiscent of the interactions between calmodulin and its target peptides. Site-specific mutagenesis combined with functional characterization shows that those interactions mediated by alpha1 and H10 are essential to the modulation of Kv4.2 by KChIPs.

PubMed: 14980206
DOI: 10.1016/S0896-6273(04)00045-5

実験手法

X-RAY DIFFRACTION (2 Å)