1ZTN

INACTIVATION GATE OF POTASSIUM CHANNEL RAW3, NMR, 8 STRUCTURES

1ZTN の概要

• エントリーDOI: 10.2210/pdb1ztn/pdb
• 分子名称: Potassium voltage-gated channel subfamily C member 4 (1 entity in total)
• 機能のキーワード: potassium channel, inactivation gate, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Multi-pass membrane protein: Q03721
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 3280.86

構造登録者

Antz, C.,Geyer, M.,Fakler, B.,Schott, M.,Frank, R.,Guy, H.R.,Ruppersberg, J.P.,Kalbitzer, H.R. (登録日: 1996-11-15, 公開日: 1997-06-05, 最終更新日: 2024-05-01)

主引用文献

Antz, C.,Geyer, M.,Fakler, B.,Schott, M.K.,Guy, H.R.,Frank, R.,Ruppersberg, J.P.,Kalbitzer, H.R.
NMR structure of inactivation gates from mammalian voltage-dependent potassium channels.
Nature, 385:272-275, 1997

PubMed Abstract: The electrical signalling properties of neurons originate largely from the gating properties of their ion channels. N-type inactivation of voltage-gated potassium (Kv) channels is the best-understood gating transition in ion channels, and occurs by a 'ball-and-chain' type mechanism. In this mechanism an N-terminal domain (inactivation gate), which is tethered to the cytoplasmic side of the channel protein by a protease-cleavable chain, binds to its receptor at the inner vestibule of the channel, thereby physically blocking the pore. Even when synthesized as a peptide, ball domains restore inactivation in Kv channels whose inactivation domains have been deleted. Using high-resolution nuclear magnetic resonance (NMR) spectroscopy, we analysed the three-dimensional structure of the ball peptides from two rapidly inactivating mammalian K. channels (Raw3 (Kv3.4) and RCK4 (Kv1.4)). The inactivation peptide of Raw3 (Raw3-IP) has a compact structure that exposes two phosphorylation sites and allows the formation of an intramolecular disulphide bridge between two spatially close cysteine residues. Raw3-IP exhibits a characteristic surface charge pattern with a positively charged, a hydrophobic, and a negatively charged region. The RCK4 inactivation peptide (RCK4-IP) shows a similar spatial distribution of charged and uncharged regions, but is more flexible and less ordered in its amino-terminal part.

PubMed: 9000078
DOI: 10.1038/385272a0

実験手法

SOLUTION NMR