1KN7

Solution structure of the tandem inactivation domain (residues 1-75) of potassium channel RCK4 (Kv1.4)

1KN7 の概要

• エントリーDOI: 10.2210/pdb1kn7/pdb
• 関連するPDBエントリー: 1zto
• NMR情報: BMRB: 5236
• 分子名称: VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN KV1.4 (1 entity in total)
• 機能のキーワード: voltage-gated potassium channel, inactivation domain, kv1.4, rck4, membrane protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P15385
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7858.49

構造登録者

Wissmann, R.,Bildl, W.,Oliver, D.,Beyermann, M.,Kalbitzer, H.R.,Bentrop, D.,Fakler, B. (登録日: 2001-12-18, 公開日: 2003-05-06, 最終更新日: 2024-05-22)

主引用文献

Wissmann, R.,Bildl, W.,Oliver, D.,Beyermann, M.,Kalbitzer, H.R.,Bentrop, D.,Fakler, B.
Solution Structure and Function of the "Tandem Inactivation Domain" of the Neuronal A-type Potassium Channel Kv1.4
J.Biol.Chem., 278:16142-16150, 2003

PubMed Abstract: Cumulative inactivation of voltage-gated (Kv) K(+) channels shapes the presynaptic action potential and determines timing and strength of synaptic transmission. Kv1.4 channels exhibit rapid "ball-and-chain"-type inactivation gating. Different from all other Kvalpha subunits, Kv1.4 harbors two inactivation domains at its N terminus. Here we report the solution structure and function of this "tandem inactivation domain" using NMR spectroscopy and patch clamp recordings. Inactivation domain 1 (ID1, residues 1-38) consists of a flexible N terminus anchored at a 5-turn helix, whereas ID2 (residues 40-50) is a 2.5-turn helix made up of small hydrophobic amino acids. Functional analysis suggests that only ID1 may work as a pore-occluding ball domain, whereas ID2 most likely acts as a "docking domain" that attaches ID1 to the cytoplasmic face of the channel. Deletion of ID2 slows inactivation considerably and largely impairs cumulative inactivation. Together, the concerted action of ID1 and ID2 may promote rapid inactivation of Kv1.4 that is crucial for the channel function in short term plasticity.

PubMed: 12590144
DOI: 10.1074/jbc.M210191200

実験手法

SOLUTION NMR