3MT5
Crystal Structure of the Human BK Gating Apparatus
3MT5 の概要
エントリーDOI | 10.2210/pdb3mt5/pdb |
分子名称 | Potassium large conductance calcium-activated channel, subfamily M, alpha member 1, CALCIUM ION, SULFATE ION (3 entities in total) |
機能のキーワード | potassium channel, membrane protein, transport protein |
由来する生物種 | Homo sapiens (human) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 81780.55 |
構造登録者 | |
主引用文献 | Yuan, P.,Leonetti, M.D.,Pico, A.R.,Hsiung, Y.,MacKinnon, R. Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution. Science, 329:182-186, 2010 Cited by PubMed Abstract: High-conductance voltage- and Ca2+-activated K+ (BK) channels encode negative feedback regulation of membrane voltage and Ca2+ signaling, playing a central role in numerous physiological processes. We determined the x-ray structure of the human BK Ca2+ gating apparatus at a resolution of 3.0 angstroms and deduced its tetrameric assembly by solving a 6 angstrom resolution structure of a Na+-activated homolog. Two tandem C-terminal regulator of K+ conductance (RCK) domains from each of four channel subunits form a 350-kilodalton gating ring at the intracellular membrane surface. A sequence of aspartic amino acids that is known as the Ca2+ bowl, and is located within the second of the tandem RCK domains, creates four Ca2+ binding sites on the outer perimeter of the gating ring at the "assembly interface" between RCK domains. Functionally important mutations cluster near the Ca2+ bowl, near the "flexible interface" between RCK domains, and on the surface of the gating ring that faces the voltage sensors. The structure suggests that the Ca2+ gating ring, in addition to regulating the pore directly, may also modulate the voltage sensor. PubMed: 20508092DOI: 10.1126/science.1190414 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3 Å) |
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