Visualization of the redox condition in activating cells
Project/Area Number |
23659111
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Research Category |
Grant-in-Aid for Challenging Exploratory Research
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Allocation Type | Multi-year Fund |
Research Field |
General physiology
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Research Institution | Osaka University |
Principal Investigator |
FUJIWARA YUICHIRO 大阪大学, 医学(系)研究科(研究院), 准教授 (20532980)
|
Project Period (FY) |
2011 – 2012
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥3,770,000 (Direct Cost: ¥2,900,000、Indirect Cost: ¥870,000)
Fiscal Year 2012: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2011: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
|
Keywords | イオンチャネル / レドックス / 電位依存性チャネル |
Research Abstract |
Oxidation is an important biochemical defense mechanism, but it also elicits toxicity; therefore, oxidation must be under strict control. In phagocytotic events in neutrophils, the voltage-gated H+ channel is a key regulator of the production of reactive oxygen species against invading bacteria. In this study, we solved the crystal structure of the cytoplasmic coiled-coil domain of the voltage-gated H+ channel in reduced, oxidized and mutated (Cys to Ser) states. The crystal structures indicated that a pair of Cys residues in the dimeric coiled-coil forms an intersubunit disulfide bond dependent on the redox conditions. Circular dichroism spectroscopy revealed that the disulfide bond increased the thermal stability of the coiled-coil protein. Thus, we revealed that the voltage-gated H+ channel has a redox-sensor in the cytoplasmic domain. We also tried to monitor the redox condition using the coiled-coil in cells.
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Report
(4 results)
Research Products
(57 results)
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[Presentation] X-RAY CRYSTAL STRUCTURE OF VOLTAGE GATED PROTON CHANNEL2014
Author(s)
竹下浩平, 坂田宗平, 山下栄樹, 藤原祐一郎, 川鍋陽, 黒川竜紀, 大河内善史, 松田真, 成田宏隆, 岡村康司, 中川敦史
Organizer
第58回米国生物物理学会大会
Place of Presentation
San Francisco(米国)
Year and Date
2014-02-19
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