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-Structure paper
タイトル | Structure of the mouse TRPC4 ion channel. |
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ジャーナル・号・ページ | Nat Commun, Vol. 9, Issue 1, Page 3102, Year 2018 |
掲載日 | 2018年8月6日 |
著者 | Jingjing Duan / Jian Li / Bo Zeng / Gui-Lan Chen / Xiaogang Peng / Yixing Zhang / Jianbin Wang / David E Clapham / Zongli Li / Jin Zhang / |
PubMed 要旨 | Members of the transient receptor potential (TRP) ion channels conduct cations into cells. They mediate functions ranging from neuronally mediated hot and cold sensation to intracellular organellar ...Members of the transient receptor potential (TRP) ion channels conduct cations into cells. They mediate functions ranging from neuronally mediated hot and cold sensation to intracellular organellar and primary ciliary signaling. Here we report a cryo-electron microscopy (cryo-EM) structure of TRPC4 in its unliganded (apo) state to an overall resolution of 3.3 Å. The structure reveals a unique architecture with a long pore loop stabilized by a disulfide bond. Beyond the shared tetrameric six-transmembrane fold, the TRPC4 structure deviates from other TRP channels with a unique cytosolic domain. This unique cytosolic N-terminal domain forms extensive aromatic contacts with the TRP and the C-terminal domains. The comparison of our structure with other known TRP structures provides molecular insights into TRPC4 ion selectivity and extends our knowledge of the diversity and evolution of the TRP channels. |
リンク | Nat Commun / PubMed:30082700 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 3.28 Å |
構造データ | |
化合物 | ChemComp-Y01: ChemComp-LPP: ChemComp-NA: |
由来 |
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キーワード | MEMBRANE PROTEIN / CryoEM / mouse full length TRPC4 |