Structural study of reconstitued full length PKC
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 |
Research Field |
Structural biochemistry
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Research Institution | Tokyo Metropolitan University |
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 |
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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Report
(3 results)
Research Products
(26 results)
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[Journal Article] Evaluation of the reliability of the maximum entropy method for reconstructing 3D and 4D NOESY-type NMR spectra of proteins.2015
Author(s)
Shigemitsu, Y., Ikeya, T., Yamamoto, A., Tsuchie, Y., Mishima, M., Smith, B. O., Guentert, P. & Ito, Y.
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Journal Title
Biochem. Biophys. Res. Commun.
Volume: 457
Issue: 2
Pages: 200-205
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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[Journal Article] Efficient and cost effective production of active-form human PKB using silkworm larvae.2014
Author(s)
R. Maesaki, R. Satoh, M. Taoka, T. Kanaba, T. Asano, C. Fujita, T. Fujiwara, Y. Ito, T. isobe, T. Hakoshima, K. Maenaka, and M. Mishima
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Journal Title
Scientific Reports
Volume: 4
Issue: 1
Pages: 6016-6016
DOI
Related Report
Peer Reviewed / Open Access
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[Journal Article] High-resolution heteronuclear multidimensional NMR of proteins living insect cells using a baculovirus protein expression system ≪2013
Author(s)
Jumpei Hamatsu, Daniel O'Donovan, Takashi Tanaka, Takahiro Shirai, Yuichiro Hourai, Tsutomu Mikawa, Teppei Ikeya, Masaki Mishima, Wayne Boucher, Brian O. Smith, Ernest D. Laue, Masahiro Shirakawa, Yutaka Ito 4
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Journal Title
Journal of the American Chemical Society
Volume: 135
Issue: 5
Pages: 1688-1691
DOI
Related Report
Peer Reviewed
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[Journal Article] An in-cell NMR study of monitoring stress-induced increase of cytosolic Ca2+ concentration in HeLa cells2013
Author(s)
Dambarudhar Shiba Sankar Hembrama, Takahiro Haremakia, Jumpei Hamatsua, Jin Inouea, Hajime Kamoshidaa, Teppei Ikeyaa, Masaki Mishimaa, Tsutomu Mikawab, Nobuhiro Hayashic, Masahiro Shirakawad, Yutaka Ito
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Journal Title
Biochem Biophys Res Commun
Volume: 438
Issue: 4
Pages: 653-659
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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