| Project/Area Number |
25650025
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Tokyo Metropolitan University |
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Principal Investigator |
MISHIMA Masaki 首都大学東京, 理工学研究科, 准教授 (70346310)
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| Co-Investigator(Renkei-kenkyūsha) |
ITO Yutaka 首都大学東京, 大学院・理工学研究科, 教授 (80261147)
HIRAI Go 独立行政法人理化学研究所, 専任研究員 (50359551)
SODEOKA Mikiko 独立行政法人理化学研究所, 主任研究員 (60192142)
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| Project Period (FY) |
2013-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
Fiscal Year 2013: ¥2,470,000 (Direct Cost: ¥1,900,000、Indirect Cost: ¥570,000)
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| Keywords | NMR / マルチドメインタンパク質 / sortase / プロテインライゲーション / PKC / 構造解析 / 活性制御 |
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| Outline of Final Research Achievements |
Protein kinase C (PKC) family is a multi-domain protein consists of N-terminal regulatory domains (C1 and C2 domain) and C-terminal kinase domain, and regulates a wide range of biological processes. In cytoplasm, PKC is thought to be autoinhibited by the interaction between regulatory domains and the kinase domain. Recently, the full-length crystal structure of PKCbII was reported. However, in this crystal structure, the C1A domain was not observed and the C2 domain was influenced by the crystal packing interaction. Therefore, the domain orientation and the interactions between the domains of PKC are still elusive. In this study, we are trying to determine the structures of full-length PKC proteins, PKCalpha and PKCtheta, and investigate the regulation mechanism using long-range distance information derived from PRE detected by solution hetero-nuclear NMR.
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