- EMDB-20192: Structure of the TRPV3 K169A sensitized mutant in apo form at 4.1... -
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基本情報
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データベース: EMDB / ID: EMD-20192
タイトル
Structure of the TRPV3 K169A sensitized mutant in apo form at 4.1 A resolution.
マップデータ
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試料
複合体: Human TRPV3 ion channel
タンパク質・ペプチド: Transient receptor potential cation channel subfamily V member 3
キーワード
Ion channel (イオンチャネル) / TRP channel (TRPチャネル) / TRPV channel / Metal transport / Membrane transport / membrane protein (膜タンパク質) / TRANSPORT PROTEIN (運搬体タンパク質)
機能・相同性
機能・相同性情報
negative regulation of hair cycle / osmosensory signaling pathway / TRPチャネル / response to temperature stimulus / positive regulation of calcium ion import / calcium ion import across plasma membrane / actin filament organization / calcium ion transmembrane transport / calcium channel activity / 繊毛 ...negative regulation of hair cycle / osmosensory signaling pathway / TRPチャネル / response to temperature stimulus / positive regulation of calcium ion import / calcium ion import across plasma membrane / actin filament organization / calcium ion transmembrane transport / calcium channel activity / 繊毛 / receptor complex / identical protein binding / 細胞膜 類似検索 - 分子機能
Transient receptor potential cation channel subfamily V member 1-4 / Transient receptor potential cation channel subfamily V / Ankyrin repeat / Ankyrin repeats (3 copies) / Ankyrin repeat profile. / Ankyrin repeat region circular profile. / ankyrin repeats / Ankyrin repeat / Ankyrin repeat-containing domain superfamily / Ion transport domain / Ion transport protein 類似検索 - ドメイン・相同性
Transient receptor potential cation channel subfamily V member 3 類似検索 - 構成要素
National Institutes of Health/National Institute of Neurological Disorders and Stroke (NIH/NINDS)
R35NS097241
米国
National Institutes of Health/National Institute of Environmental Health Sciences (NIH/NIEHS)
ZIC ES103326
米国
引用
ジャーナル: Elife / 年: 2019 タイトル: Regulatory switch at the cytoplasmic interface controls TRPV channel gating. 著者: Lejla Zubcevic / William F Borschel / Allen L Hsu / Mario J Borgnia / Seok-Yong Lee / 要旨: Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess ...Temperature-sensitive transient receptor potential vanilloid (thermoTRPV) channels are activated by ligands and heat, and are involved in various physiological processes. ThermoTRPV channels possess a large cytoplasmic ring consisting of N-terminal ankyrin repeat domains (ARD) and C-terminal domains (CTD). The cytoplasmic inter-protomer interface is unique and consists of a CTD coiled around a β-sheet which makes contacts with the neighboring ARD. Despite much existing evidence that the cytoplasmic ring is important for thermoTRPV function, the mechanism by which this unique structure is involved in thermoTRPV gating has not been clear. Here, we present cryo-EM and electrophysiological studies which demonstrate that TRPV3 gating involves large rearrangements at the cytoplasmic inter-protomer interface and that this motion triggers coupling between cytoplasmic and transmembrane domains, priming the channel for opening. Furthermore, our studies unveil the role of this interface in the distinct biophysical and physiological properties of individual thermoTRPV subtypes.