Loading
PDBj
メニューPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

5TJI

Ca2+ bound aplysia Slo1

5TJI の概要
エントリーDOI10.2210/pdb5tji/pdb
関連するPDBエントリー5TJ6
EMDBエントリー8410 8414
分子名称High conductance calcium-activated potassium channel, (1R)-2-{[(S)-{[(2S)-2,3-dihydroxypropyl]oxy}(hydroxy)phosphoryl]oxy}-1-[(hexadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate (2 entities in total)
機能のキーワードion channel, k+ channel, ca2+ bound, high conductance, membrane protein
由来する生物種Aplysia californica (California sea hare)
タンパク質・核酸の鎖数1
化学式量合計121057.01
構造登録者
MacKinnon, R.,Tao, X.,Hite, R.K. (登録日: 2016-10-04, 公開日: 2016-12-28, 最終更新日: 2024-03-13)
主引用文献Hite, R.K.,Tao, X.,MacKinnon, R.
Structural basis for gating the high-conductance Ca(2+)-activated K(+) channel.
Nature, 541:52-57, 2017
Cited by
PubMed Abstract: The precise control of an ion channel gate by environmental stimuli is crucial for the fulfilment of its biological role. The gate in Slo1 K channels is regulated by two separate stimuli, intracellular Ca concentration and membrane voltage. Slo1 is thus central to understanding the relationship between intracellular Ca and membrane excitability. Here we present the Slo1 structure from Aplysia californica in the absence of Ca and compare it with the Ca-bound channel. We show that Ca binding at two unique binding sites per subunit stabilizes an expanded conformation of the Ca sensor gating ring. These conformational changes are propagated from the gating ring to the pore through covalent linkers and through protein interfaces formed between the gating ring and the voltage sensors. The gating ring and the voltage sensors are directly connected through these interfaces, which allow membrane voltage to regulate gating of the pore by influencing the Ca sensors.
PubMed: 27974801
DOI: 10.1038/nature20775
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.8 Å)
構造検証レポート
Validation report summary of 5tji
検証レポート(詳細版)ダウンロードをダウンロード

226707

件を2024-10-30に公開中

PDB statisticsPDBj update infoContact PDBjnumon