Structural basis for the reguration mechanism of MAP kinase activity

2016 Fiscal Year Final Research Report

• Project/Area Number: 26440035
• Research Category: Grant-in-Aid for Scientific Research (C)
• Allocation Type: Multi-year Fund
• Section: 一般
• Research Field: Structural biochemistry
• Research Institution: Osaka Prefecture University
• Principal Investigator: Tada Toshiji 大阪府立大学, 理学(系)研究科(研究院), 客員研究員 (70275288)
• Co-Investigator(Renkei-kenkyūsha): NAKAE SETSU 長浜バイオ大学, コンピュータバイオサイエンス学科, 助手 (10749352)
• Project Period (FY): 2014-04-01 – 2017-03-31
• Keywords: タンパク質結晶学 / MAPキナーゼ / MEK / 活性制御機構

Outline of Final Research Achievements

A protein kinase activity is regulated by phosphorylation in several amino acids. The aim of this work is to elucidate the molecular mechanism of MEK1 by analyzing its crystal structures of non-phosphorylated body, active mutant, S212-inactive mutant. Diffraction data sets were collected at the BL38B1 station of SPring-8. The knowledge obtained from these structures are as follows: divalent cation responsible for the conformation of DFG-motif, the increment of flexibility of active segment leads a change to active conformation, and phosphorylation of S212 disturbs the binding of ATP.

Free Research Field

構造生物学