2011 Fiscal Year Final Research Report
Structural basis of a novel Wnt signaling regulation by dynamic oligomerized proteins
Project/Area Number |
22770112
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Structural biochemistry
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Research Institution | Gunma University (2011) University of Hyogo (2010) |
Principal Investigator |
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Project Period (FY) |
2010 – 2011
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Keywords | 動的オリゴマー形成 / Wntシグナル伝達 / DIXドメイン |
Research Abstract |
The Wnt signaling pathway plays an essential role in cell growth, differentiation, polarity formation and neural development. Coiled-Coil DIX1 (CCD1) and Axin have a novel ability to form dynamic oligomers and the complex formation. To elucidate the interaction between CCD1 and Axin, we have been carried out structural studies of the CCD1-Axin complex using X-ray crystallography. We established the preparation of the DIX domains of both proteins, which are necessary for the dynamic oligomerization and the complex formation. We performed crystallization trials on the CCD1-Axin complex. The crystals were unsuitable for crystallographic analysis because their diffraction quality was poor (around 20 Å).Improvement of the crystallization condition is required for the structural analysis of the CCD1-Axin complex.
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[Journal Article] Crystallographic characterization of the DIX domain of the Wnt signalling positive regulator Ccd1.2011
Author(s)
Terawaki, S., Yano, K., Katsutani, T., Shiomi, K., Keino-Masu, K., Masu, M., Shomura, Y., Komori, H., Shibata, N. Higuchi Y.
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Journal Title
Acta Crystallogr. Sect F Struct. Biol. Cryst. Commun.
Volume: 67
Pages: 758-761
Peer Reviewed
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