7LJ5

Human TRAAK K+ channel FHIEG mutant A198E in a K+ bound conductive conformation

7LJ5 の概要

• エントリーDOI: 10.2210/pdb7lj5/pdb
• 分子名称: Isoform 2 of Potassium channel subfamily K member 4, ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT LIGHT CHAIN, ANTI-TRAAK ANTIBODY 13E9 FAB FRAGMENT HEAVY CHAIN, ... (6 entities in total)
• 機能のキーワード: potassium ion channel, metal transport, metal transport-immune system complex, metal transport/immune system
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 158674.86

構造登録者

Rietmeijer, R.A.,Brohawn, S.G. (登録日: 2021-01-28, 公開日: 2021-06-30, 最終更新日: 2024-11-20)

主引用文献

Rietmeijer, R.A.,Sorum, B.,Li, B.,Brohawn, S.G.
Physical basis for distinct basal and mechanically gated activity of the human K + channel TRAAK.
Neuron, 109:2902-2913.e4, 2021

PubMed Abstract: TRAAK is a mechanosensitive two-pore domain K (K2P) channel localized to nodes of Ranvier in myelinated neurons. TRAAK deletion in mice results in mechanical and thermal allodynia, and gain-of-function mutations cause the human neurodevelopmental disorder FHEIG. TRAAK displays basal and stimulus-gated activities typical of K2Ps, but the mechanistic and structural differences between these modes are unknown. Here, we demonstrate that basal and mechanically gated openings are distinguished by their conductance, kinetics, and structure. Basal openings are low conductance, short duration, and due to a conductive channel conformation with the interior cavity exposed to the surrounding membrane. Mechanically gated openings are high conductance, long duration, and due to a channel conformation in which the interior cavity is sealed to the surrounding membrane. Our results explain how dual modes of activity are produced by a single ion channel and provide a basis for the development of state-selective pharmacology with the potential to treat disease.

PubMed: 34390650
DOI: 10.1016/j.neuron.2021.07.009

実験手法

X-RAY DIFFRACTION (2.26 Å)