- EMDB-7299: 3.7 angstrom cryoEM structure of full length human TRPM4 -
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基本情報
登録情報
データベース: EMDB / ID: EMD-7299
タイトル
3.7 angstrom cryoEM structure of full length human TRPM4
マップデータ
試料
複合体: Human full length TRPM4
タンパク質・ペプチド: Transient receptor potential cation channel subfamily M member 4
リガンド: SODIUM ION
リガンド: CHOLESTEROL HEMISUCCINATE
リガンド: 2-acetamido-2-deoxy-beta-D-glucopyranose
キーワード
CryoEM / human full length TRPM7 / MEMBRANE PROTEIN
機能・相同性
機能・相同性情報
positive regulation of atrial cardiac muscle cell action potential / positive regulation of regulation of vascular associated smooth muscle cell membrane depolarization / sodium channel complex / regulation of T cell cytokine production / membrane depolarization during AV node cell action potential / metal ion transport / membrane depolarization during bundle of His cell action potential / membrane depolarization during Purkinje myocyte cell action potential / negative regulation of bone mineralization / regulation of ventricular cardiac muscle cell action potential ...positive regulation of atrial cardiac muscle cell action potential / positive regulation of regulation of vascular associated smooth muscle cell membrane depolarization / sodium channel complex / regulation of T cell cytokine production / membrane depolarization during AV node cell action potential / metal ion transport / membrane depolarization during bundle of His cell action potential / membrane depolarization during Purkinje myocyte cell action potential / negative regulation of bone mineralization / regulation of ventricular cardiac muscle cell action potential / calcium-activated cation channel activity / sodium ion import across plasma membrane / inorganic cation transmembrane transport / dendritic cell chemotaxis / TRP channels / cellular response to ATP / sodium channel activity / monoatomic cation transmembrane transport / regulation of heart rate by cardiac conduction / positive regulation of insulin secretion involved in cellular response to glucose stimulus / protein sumoylation / negative regulation of osteoblast differentiation / positive regulation of fat cell differentiation / positive regulation of heart rate / positive regulation of adipose tissue development / positive regulation of vasoconstriction / calcium-mediated signaling / calcium ion transmembrane transport / calcium channel activity / Sensory perception of sweet, bitter, and umami (glutamate) taste / positive regulation of canonical Wnt signaling pathway / positive regulation of cytosolic calcium ion concentration / protein homotetramerization / adaptive immune response / calmodulin binding / neuronal cell body / positive regulation of cell population proliferation / calcium ion binding / endoplasmic reticulum / Golgi apparatus / nucleoplasm / ATP binding / identical protein binding / membrane / plasma membrane 類似検索 - 分子機能
TRPM, SLOG domain / : / SLOG in TRPM / Ion transport domain / Ion transport protein 類似検索 - ドメイン・相同性
Transient receptor potential cation channel subfamily M member 4 類似検索 - 構成要素
ジャーナル: Proc Natl Acad Sci U S A / 年: 2018 タイトル: Structure of full-length human TRPM4. 著者: Jingjing Duan / Zongli Li / Jian Li / Ana Santa-Cruz / Silvia Sanchez-Martinez / Jin Zhang / David E Clapham / 要旨: Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in ...Transient receptor potential melastatin subfamily member 4 (TRPM4) is a widely distributed, calcium-activated, monovalent-selective cation channel. Mutations in human TRPM4 (hTRPM4) result in progressive familial heart block. Here, we report the electron cryomicroscopy structure of hTRPM4 in a closed, Na-bound, apo state at pH 7.5 to an overall resolution of 3.7 Å. Five partially hydrated sodium ions are proposed to occupy the center of the conduction pore and the entrance to the coiled-coil domain. We identify an upper gate in the selectivity filter and a lower gate at the entrance to the cytoplasmic coiled-coil domain. Intramolecular interactions exist between the TRP domain and the S4-S5 linker, N-terminal domain, and N and C termini. Finally, we identify aromatic interactions via π-π bonds and cation-π bonds, glycosylation at an N-linked extracellular site, a pore-loop disulfide bond, and 24 lipid binding sites. We compare and contrast this structure with other TRP channels and discuss potential mechanisms of regulation and gating of human full-length TRPM4.