Molecular basis regulating multiple signals by an adaptor protein
| Project/Area Number |
24770087
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Hokkaido University |
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Principal Investigator |
OSE TOYOYUKI 北海道大学, 薬学研究科(研究院), 准教授 (80380525)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,680,000 (Direct Cost: ¥3,600,000、Indirect Cost: ¥1,080,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥3,510,000 (Direct Cost: ¥2,700,000、Indirect Cost: ¥810,000)
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| Keywords | シグナル伝達 / 構造生物 / タンパク質 / X線結晶構造解析 / 分子間相互作用 / アダプター蛋白質 |
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| Research Abstract |
The non-receptor tyrosine kinase breast tumor kinase (Brk), also known as PTK6, has been identified as a highly expressed Protein-tyrosine kinases in human melanocyte.
STAP-2 is also known as breast tumor kinase (Brk) substrate (BKS). it is important to better understand the contribution of Brk kinase activity and protein interactions to the STAT3-mediated signal transduction pathways in breast cancer. Brk phosphorylates STAP-2 and phosphorylated STAP-2 is believed to play an important role in Brk-mediated STAT3 activation. We purified Brk, STAP-2, and STAT3 and checked the kinase activity in vitro. Using purified proteins, we also checked the binding affinity between Brk and STAP-2. The information obtained by small angle xray scattering (SAXS) experiments was also useful to judge whether the conformational change of Brk is included (open/closed).
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Report
(3 results)
Research Products
(3 results)
