6XIT

Cryo-EM structure of the G protein-gated inward rectifier K+ channel GIRK2 (Kir3.2) in complex with PIP2

6XIT の概要

• エントリーDOI: 10.2210/pdb6xit/pdb
• 関連するPDBエントリー: 6XIS
• EMDBエントリー: 22199 22200
• 分子名称: G protein-activated inward rectifier potassium channel 2, [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate, POTASSIUM ION (3 entities in total)
• 機能のキーワード: g protein-coupled inwardly rectifying potassium channels, pip2, membrane protein
• 由来する生物種: Mus musculus (Mouse)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 159351.39

構造登録者

Niu, Y.,Tao, X.,MacKinnon, R. (登録日: 2020-06-21, 公開日: 2020-10-07, 最終更新日: 2024-10-23)

主引用文献

Niu, Y.,Tao, X.,Touhara, K.K.,MacKinnon, R.
Cryo-EM analysis of PIP 2 regulation in mammalian GIRK channels.
Elife, 9:-, 2020

PubMed Abstract: G-protein-gated inward rectifier potassium (GIRK) channels are regulated by G proteins and PIP. Here, using cryo-EM single particle analysis we describe the equilibrium ensemble of structures of neuronal GIRK2 as a function of the C8-PIP concentration. We find that PIP shifts the equilibrium between two distinguishable structures of neuronal GIRK (GIRK2), extended and docked, towards the docked form. In the docked form the cytoplasmic domain, to which G binds, becomes accessible to the cytoplasmic membrane surface where G resides. Furthermore, PIP binding reshapes the G binding surface on the cytoplasmic domain, preparing it to receive G. We find that cardiac GIRK (GIRK1/4) can also exist in both extended and docked conformations. These findings lead us to conclude that PIP influences GIRK channels in a structurally similar manner to Kir2.2 channels. In Kir2.2 channels, the PIP-induced conformational changes open the pore. In GIRK channels, they prepare the channel for activation by G.

PubMed: 32844743
DOI: 10.7554/eLife.60552

実験手法

ELECTRON MICROSCOPY (3.3 Å)