| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2016: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2015: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2014: ¥1,690,000 (Direct Cost: ¥1,300,000、Indirect Cost: ¥390,000)
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| 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.
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