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2014 Fiscal Year Final Research Report

Structural study of reconstitued full length PKC

Research Project

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Project/Area Number 25650025
Research Category

Grant-in-Aid for Challenging Exploratory Research

Allocation TypeMulti-year Fund
Research Field Structural biochemistry
Research InstitutionTokyo Metropolitan University

Principal Investigator

MISHIMA Masaki  首都大学東京, 理工学研究科, 准教授 (70346310)

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)
Project Period (FY) 2013-04-01 – 2015-03-31
KeywordsNMR / 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
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.

Free Research Field

構造生物化学

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Published: 2016-09-02  

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