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-Structure paper
タイトル | Structure of the human TRPM4 ion channel in a lipid nanodisc. |
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ジャーナル・号・ページ | Science, Vol. 359, Issue 6372, Page 228-232, Year 2018 |
掲載日 | 2018年1月12日 |
著者 | Henriette E Autzen / Alexander G Myasnikov / Melody G Campbell / Daniel Asarnow / David Julius / Yifan Cheng / |
PubMed 要旨 | Transient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular ...Transient receptor potential (TRP) melastatin 4 (TRPM4) is a widely expressed cation channel associated with a variety of cardiovascular disorders. TRPM4 is activated by increased intracellular calcium in a voltage-dependent manner but, unlike many other TRP channels, is permeable to monovalent cations only. Here we present two structures of full-length human TRPM4 embedded in lipid nanodiscs at ~3-angstrom resolution, as determined by single-particle cryo-electron microscopy. These structures, with and without calcium bound, reveal a general architecture for this major subfamily of TRP channels and a well-defined calcium-binding site within the intracellular side of the S1-S4 domain. The structures correspond to two distinct closed states. Calcium binding induces conformational changes that likely prime the channel for voltage-dependent opening. |
リンク | Science / PubMed:29217581 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.1 - 3.2 Å |
構造データ | |
化合物 | ChemComp-Y01: ChemComp-CA: |
由来 |
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キーワード | MEMBRANE PROTEIN / TRPM4 / TRPM channel / TRP channel |