Structure changs in transport sites by phosphoenzyme isomerization of sarcoplasmic reticulum Ca2+ pump
| Project/Area Number |
23570130
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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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| Research Field |
Structural biochemistry
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| Research Institution | Asahikawa Medical College |
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Principal Investigator |
DAIHO Takashi 旭川医科大学, 医学部, 准教授 (90207267)
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| Project Period (FY) |
2011 – 2013
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥5,460,000 (Direct Cost: ¥4,200,000、Indirect Cost: ¥1,260,000)
Fiscal Year 2013: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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)
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| Keywords | カルシウムポンプ / 小胞体 / リン酸化中間体 / カチオン輸送 / 部位特異的変異 / gate / ドメイン / ATPアーゼ / Ca2+-ATPase / エネルギー共役 / カチオン能動輸送 / 筋小胞体 / ATPase / カルシウム / 異性化 / P型ATPase / Ca2+ |
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| Research Abstract |
Ca2+ pump forms phosphorylated intermediates (EP) in Ca2+ transport cycle.In EP isomerization structural changes in cytoplasmic domains are transmitted to the Ca2+ sites in the membrane domain to tranlocate Ca2+ into lumen.Functional roles of helix M2 and its linker with the cytoplasmic Actuator-domain are explored by mutation study.The results show that each portion of M2 and its linker function in coupling of ATP hydrolysis and Ca2+ transport,EP hydrolysis, open-close of cytoplasmic and luminal Ca2+-gate,and Ca2+-induced activation of unphosphorylated intermediate.Therefore,the structural changes of M2 and its linker play critical roles region-specifically and step-specifically, and thereby couple the structural events in the catalytic site and the transport sites for the Ca2+ transport.
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Report
(4 results)
Research Products
(30 results)
