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3UM7

Crystal structure of the human two pore domain K+ ion channel TRAAK (K2P4.1)

3UM7 の概要
エントリーDOI10.2210/pdb3um7/pdb
分子名称Potassium channel subfamily K member 4, POTASSIUM ION (2 entities in total)
機能のキーワードpotassium ion channel, metal transport
由来する生物種Homo sapiens (human)
細胞内の位置Membrane; Multi-pass membrane protein (Potential): Q9NYG8
タンパク質・核酸の鎖数2
化学式量合計67367.10
構造登録者
Brohawn, S.G.,MacKinnon, R. (登録日: 2011-11-12, 公開日: 2012-02-08)
主引用文献Brohawn, S.G.,del Marmol, J.,MacKinnon, R.
Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channel.
Science, 335:436-441, 2012
Cited by
PubMed Abstract: TRAAK channels, members of the two-pore domain K(+) (potassium ion) channel family K2P, are expressed almost exclusively in the nervous system and control the resting membrane potential. Their gating is sensitive to polyunsaturated fatty acids, mechanical deformation of the membrane, and temperature changes. Physiologically, these channels appear to control the noxious input threshold for temperature and pressure sensitivity in dorsal root ganglia neurons. We present the crystal structure of human TRAAK at a resolution of 3.8 angstroms. The channel comprises two protomers, each containing two distinct pore domains, which create a two-fold symmetric K(+) channel. The extracellular surface features a helical cap, 35 angstroms tall, that creates a bifurcated pore entryway and accounts for the insensitivity of two-pore domain K(+) channels to inhibitory toxins. Two diagonally opposed gate-forming inner helices form membrane-interacting structures that may underlie this channel's sensitivity to chemical and mechanical properties of the cell membrane.
PubMed: 22282805
DOI: 10.1126/science.1213808
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (3.31 Å)
構造検証レポート
Validation report summary of 3um7
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2024-11-13に公開中

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