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-Structure paper
タイトル | Structures of the calcium-activated, non-selective cation channel TRPM4. |
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ジャーナル・号・ページ | Nature, Vol. 552, Issue 7684, Page 205-209, Year 2017 |
掲載日 | 2017年12月14日 |
著者 | Jiangtao Guo / Ji She / Weizhong Zeng / Qingfeng Chen / Xiao-Chen Bai / Youxing Jiang / |
PubMed 要旨 | TRPM4 is a calcium-activated, phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P) -modulated, non-selective cation channel that belongs to the family of melastatin-related transient receptor ...TRPM4 is a calcium-activated, phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P) -modulated, non-selective cation channel that belongs to the family of melastatin-related transient receptor potential (TRPM) channels. Here we present the electron cryo-microscopy structures of the mouse TRPM4 channel with and without ATP. TRPM4 consists of multiple transmembrane and cytosolic domains, which assemble into a three-tiered architecture. The N-terminal nucleotide-binding domain and the C-terminal coiled-coil participate in the tetrameric assembly of the channel; ATP binds at the nucleotide-binding domain and inhibits channel activity. TRPM4 has an exceptionally wide filter but is only permeable to monovalent cations; filter residue Gln973 is essential in defining monovalent selectivity. The S1-S4 domain and the post-S6 TRP domain form the central gating apparatus that probably houses the Ca- and PtdIns(4,5)P-binding sites. These structures provide an essential starting point for elucidating the complex gating mechanisms of TRPM4 and reveal the molecular architecture of the TRPM family. |
リンク | Nature / PubMed:29211714 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.88 - 3.54 Å |
構造データ | EMDB-7081, PDB-6bcj: EMDB-7082, PDB-6bcl: |
化合物 | ChemComp-NA: ChemComp-HOH: ChemComp-ATP: |
由来 |
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キーワード | TRANSPORT PROTEIN / ion channel |