3UM7
Crystal structure of the human two pore domain K+ ion channel TRAAK (K2P4.1)
3UM7 の概要
エントリーDOI | 10.2210/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 | |
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: 22282805DOI: 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) |
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