5YWB

Structure of pancreatic ATP-sensitive potassium channel bound with Mg-ADP (CTD class2 at 5.2A)

5YWB の概要

• エントリーDOI: 10.2210/pdb5ywb/pdb
• EMDBエントリー: 6851
• 分子名称: ATP-sensitive inward rectifier potassium channel 11, ATP-binding cassette sub-family C member 8 isoform X2, ADENOSINE-5'-DIPHOSPHATE, ... (4 entities in total)
• 機能のキーワード: katp, channel, glibenclamide, sulfonylurea, membrane protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 888965.85

構造登録者

Chen, L.,Wu, J.X. (登録日: 2017-11-29, 公開日: 2018-05-30, 最終更新日: 2024-10-23)

主引用文献

Wu, J.X.,Ding, D.,Wang, M.,Kang, Y.,Zeng, X.,Chen, L.
Ligand binding and conformational changes of SUR1 subunit in pancreatic ATP-sensitive potassium channels.
Protein Cell, 9:553-567, 2018

PubMed Abstract: ATP-sensitive potassium channels (K) are energy sensors on the plasma membrane. By sensing the intracellular ADP/ATP ratio of β-cells, pancreatic K channels control insulin release and regulate metabolism at the whole body level. They are implicated in many metabolic disorders and diseases and are therefore important drug targets. Here, we present three structures of pancreatic K channels solved by cryo-electron microscopy (cryo-EM), at resolutions ranging from 4.1 to 4.5 Å. These structures depict the binding site of the antidiabetic drug glibenclamide, indicate how Kir6.2 (inward-rectifying potassium channel 6.2) N-terminus participates in the coupling between the peripheral SUR1 (sulfonylurea receptor 1) subunit and the central Kir6.2 channel, reveal the binding mode of activating nucleotides, and suggest the mechanism of how Mg-ADP binding on nucleotide binding domains (NBDs) drives a conformational change of the SUR1 subunit.

PubMed: 29594720
DOI: 10.1007/s13238-018-0530-y

実験手法

ELECTRON MICROSCOPY (5.2 Å)