Structural basis of Wnt signaling regulation by dynamic oligomerized proteins
| Project/Area Number |
25840017
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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 | Gunma University |
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Principal Investigator |
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| Project Period (FY) |
2013-04-01 – 2017-03-31
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| Project Status |
Completed (Fiscal Year 2016)
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| Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2015: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | Wntシグナル伝達 / 動的オリゴマー形成 / X線結晶構造解析 / Wntシグナル / DIXドメイン |
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| Outline of Final Research Achievements |
The dynamic oligomerized proteins, Coiled-coil DIX1(Ccd1) and Axin, play an important role in the regulation of the Wnt signaling pathway by forming homotypic and heterotypic oligomers between the DIX domains. The structural study for the Ccd1-Axin hetero-oligomer using X-ray crystallography reveals the heterotypic interaction of the Ccd1 DIX domain with the Axin DIX domain and a significance of the hetero-oligomerization in the regulation of the Wnt signaling pathway. This report describes the preparation, crystallization, X-ray diffraction and structural analysis of the Ccd1-Axin hetero-oligomer. The crystals of the Ccd1-Axin hetero-oligomer diffracted to a resolution of 3.1 angstrom. Structural analysis of the Ccd1-Axin hetero-oligomer is now in progress.
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Report
(5 results)
Research Products
(48 results)
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[Journal Article] Protein stabilizer, NDSB-195, enhances the dynamics of the β4-α2 loop of ubiqutin.2016
Author(s)
Wang, H., Hosoda, K., Ishii, T., Arai, R., Kohno, T., Terawaki, S. & Wakamatsu, K.
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Journal Title
J. Pept. Sci.
Volume: 22
Issue: 3
Pages: 174-180
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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