Project/Area Number |
23000014
|
Research Category |
Grant-in-Aid for Specially Promoted Research
|
Allocation Type | Single-year Grants |
Review Section |
Biological Sciences
|
Research Institution | The University of Tokyo |
Principal Investigator |
|
Co-Investigator(Kenkyū-buntansha) |
OGAWA Haruo 東京大学, 分子細胞生物学研究所, 准教授 (40292726)
MIMURA Hisatoshi 東京大学, 分子細胞生物学研究所, 助教 (30463904)
KANAI Ryuta 東京大学, 分子細胞生物学研究所, 助教 (50598472)
KABASHIMA Yoshiki 東京大学, 分子細胞生物学研究所, 助教 (00580573)
|
Research Collaborator |
Inesi Giuseppe カリフォルニアパシフィック医学センター研究所, 教授
Vilsen Bente オルフス大学, 教授
Cornelius Flemming オルフス大学, 教授
Karlish Steven ワイズマン研究所, 教授
|
Project Period (FY) |
2011 – 2016
|
Project Status |
Completed (Fiscal Year 2016)
|
Budget Amount *help |
¥519,480,000 (Direct Cost: ¥399,600,000、Indirect Cost: ¥119,880,000)
Fiscal Year 2015: ¥89,050,000 (Direct Cost: ¥68,500,000、Indirect Cost: ¥20,550,000)
Fiscal Year 2014: ¥89,050,000 (Direct Cost: ¥68,500,000、Indirect Cost: ¥20,550,000)
Fiscal Year 2013: ¥129,480,000 (Direct Cost: ¥99,600,000、Indirect Cost: ¥29,880,000)
Fiscal Year 2012: ¥105,170,000 (Direct Cost: ¥80,900,000、Indirect Cost: ¥24,270,000)
Fiscal Year 2011: ¥106,730,000 (Direct Cost: ¥82,100,000、Indirect Cost: ¥24,630,000)
|
Keywords | イオンポンプ / 膜蛋白質 / 結晶解析 / エネルギー変換 / エネルギー交換 |
Outline of Final Research Achievements |
In this project, we aimed at complete understanding of the mechanism of active transport and pursued “why the structures of ion pumps have to be so” by carrying out crystal structure analyses of Ca^<2+>- and Na^+-pumps. With the Ca^<2+>-pump, we succeeded in elucidating the long-awaited E1 crystal structure and showed the regulatory mechanism of sarcolipin, an associated regulatory protein. With the Na^+ pump, we succeeded in determining the crystal structure of a Na^+-bound form for the first time, resulting in the elucidation of an intricate mechanism for selecting Na^+. We also determined the crystal structures of the Na^+-pump with various cardiotonic steroids and thereby opened a way towards developing a tissue specific compound. Furthermore, we succeeded in visualising lipid bilayers in the crystals of Ca^<2+>-ATPase in four states and described detailed interactions with phospholipids.
|
Assessment Rating |
Verification Result (Rating)
A
|
Assessment Rating |
Result (Rating)
A: Progress in the research is steadily towards the initial goal. Expected research results are expected.
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