7S5V

Human KATP channel in open conformation, focused on SUR

7S5V の概要

• エントリーDOI: 10.2210/pdb7s5v/pdb
• 関連するPDBエントリー: 7S5T
• EMDBエントリー: 24840
• 分子名称: ATP-binding cassette sub-family C member 8, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: ion channel, katp, atp-sensitive potassium channel, membrane protein
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 178089.07

構造登録者

Zhao, C.,MacKinnon, R. (登録日: 2021-09-12, 公開日: 2021-12-01, 最終更新日: 2024-06-05)

主引用文献

Zhao, C.,MacKinnon, R.
Molecular structure of an open human K ATP channel.
Proc.Natl.Acad.Sci.USA, 118:-, 2021

PubMed Abstract: K channels are metabolic sensors that translate intracellular ATP/ADP balance into membrane excitability. The molecular composition of K includes an inward-rectifier potassium channel (Kir) and an ABC transporter-like sulfonylurea receptor (SUR). Although structures of K have been determined in many conformations, in all cases, the pore in Kir is closed. Here, we describe human pancreatic K (hK) structures with an open pore at 3.1- to 4.0-Å resolution using single-particle cryo-electron microscopy (cryo-EM). Pore opening is associated with coordinated structural changes within the ATP-binding site and the channel gate in Kir. Conformational changes in SUR are also observed, resulting in an area reduction of contact surfaces between SUR and Kir. We also observe that pancreatic hK exhibits the unique (among inward-rectifier channels) property of PIP-independent opening, which appears to be correlated with a docked cytoplasmic domain in the absence of PIP.

PubMed: 34815345
DOI: 10.1073/pnas.2112267118

実験手法

ELECTRON MICROSCOPY (3.3 Å)