| Project/Area Number |
23659111
|
|---|
| Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
| Allocation Type | Multi-year Fund |
|---|
| Research Field |
General physiology
|
|---|
| 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.
|
