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3UKM

Crystal structure of the human two pore domain potassium ion channel K2P1 (TWIK-1)

3UKM の概要
エントリーDOI10.2210/pdb3ukm/pdb
分子名称Potassium channel subfamily K member 1, UNDECANE, POTASSIUM ION, ... (4 entities in total)
機能のキーワードpotassium channel, membrane protein, eukaryotic, two-pore domain potassium channel, k2p channel, membrane
由来する生物種Homo sapiens (human)
細胞内の位置Membrane; Multi-pass membrane protein (Potential): O00180
タンパク質・核酸の鎖数4
化学式量合計128660.16
構造登録者
Long, S.B.,Miller, A.N. (登録日: 2011-11-09, 公開日: 2012-02-08, 最終更新日: 2024-10-30)
主引用文献Miller, A.N.,Long, S.B.
Crystal structure of the human two-pore domain potassium channel K2P1.
Science, 335:432-436, 2012
Cited by
PubMed Abstract: Two-pore domain potassium (K(+)) channels (K2P channels) control the negative resting potential of eukaryotic cells and regulate cell excitability by conducting K(+) ions across the plasma membrane. Here, we present the 3.4 angstrom resolution crystal structure of a human K2P channel, K2P1 (TWIK-1). Unlike other K(+) channel structures, K2P1 is dimeric. An extracellular cap domain located above the selectivity filter forms an ion pathway in which K(+) ions flow through side portals. Openings within the transmembrane region expose the pore to the lipid bilayer and are filled with electron density attributable to alkyl chains. An interfacial helix appears structurally poised to affect gating. The structure lays a foundation to further investigate how K2P channels are regulated by diverse stimuli.
PubMed: 22282804
DOI: 10.1126/science.1213274
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.4 Å)
構造検証レポート
Validation report summary of 3ukm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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