Structural basis for multimodal sensation in TRP channels
| Project/Area Number |
18K06156
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Review Section |
Basic Section 43040:Biophysics-related
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| Research Institution | Tottori University |
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Principal Investigator |
HINO Tomoya 鳥取大学, 工学研究科, 准教授 (40373360)
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| Co-Investigator(Kenkyū-buntansha) |
西澤 知宏 東京大学, 大学院理学系研究科(理学部), 助教 (80599077)
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| Project Period (FY) |
2018-04-01 – 2021-03-31
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| Project Status |
Completed (Fiscal Year 2020)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2020: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2019: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2018: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | イオンチャネル / 膜タンパク質 / X線結晶構造解析 / クライオ電子顕微鏡 / 結晶化 / クライオ電顕 / TRPチャネル |
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| Outline of Final Research Achievements |
TRP channels are cation selective ion channels that respond not only to chemical stimuli such as pungent chemicals but also to physical stimuli including temperature changes, mechanical force, and osmotic pressure. In this study, we investigated the effect of PIP2, a lipid molecule known as a regulator of TRP channel activity, on the temperature responses. From the cryo-EM analysis, we successfully constructed atomic model of mouse TRPV3 and found that the lipid molecules are bound between the pore helix and S6 helix presumed to be involved in the channel activation process. We also found the conditions for the microcrystal formation of human TRPV3 for serial femto-second X-ray crystallography.
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| Academic Significance and Societal Importance of the Research Achievements |
温度感知はほとんどの人が日常的に感じる極めて身近な生理現象である。本研究ではその感覚を引き起こす最初の段階を担うタンパク質であるTRPチャネルがどの様にして温度を感じ取るのかを原子レベルで明らかにしようという試みである。今回の結果は、脂質分子がTRPチャネルの活性化制御に重要な役割を果たすことを示唆しており、このタンパク質分子の結晶作成に成功したことも含め、今後分子レベルでの温度感知理解につながることが期待される。
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Report
(4 results)
Research Products
(9 results)
