1HO2

NMR STRUCTURE OF THE POTASSIUM CHANNEL FRAGMENT L45 IN MICELLES

1HO2 の概要

• エントリーDOI: 10.2210/pdb1ho2/pdb
• 分子名称: VOLTAGE-GATED POTASSIUM CHANNEL PROTEIN (1 entity in total)
• 機能のキーワード: alpha-helix, amphipathic, membrane protein
• 由来する生物種: Drosophila melanogaster (fruit fly)
• 細胞内の位置: Membrane; Multi-pass membrane protein: P08510
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 2200.63

構造登録者

Ohlenschlager, O.,Hojo, H.,Ramachandran, R.,Gorlach, M.,Haris, P.I. (登録日: 2000-12-08, 公開日: 2002-06-05, 最終更新日: 2024-05-22)

主引用文献

Ohlenschlager, O.,Hojo, H.,Ramachandran, R.,Gorlach, M.,Haris, P.I.
Three-dimensional structure of the S4-S5 segment of the Shaker potassium channel.
Biophys.J., 82:2995-3002, 2002

PubMed Abstract: The propagation of action potentials during neuronal signal transduction in phospholipid membranes is mediated by ion channels, a diverse group of membrane proteins. The S4-S5 linker peptide (S4-S5), that connects the S4 and S5 transmembrane segments of voltage-gated potassium channels is an important region of the Shaker ion-channel protein. Despite its importance, very little is known about its structure. Here we provide evidence for an amphipathic alpha-helical conformation of a synthetic S4-S5 peptide of the voltage-gated Drosophila melanogaster Shaker potassium channel in water/trifluoroethanol and in aqueous phospholipid micelles. The three-dimensional solution structures of the S4-S5 peptide were obtained by high-resolution nuclear magnetic resonance spectroscopy and distance-geometry/simulated-annealing calculations. The detailed structural features are discussed with respect to model studies and available mutagenesis data on the mechanism and selectivity of the potassium channel.

PubMed: 12023222

実験手法

SOLUTION NMR