Structural basis of Wnt signaling regulation by dynamic oligomerized proteins

2016 Fiscal Year Final Research Report

• Project/Area Number: 25840017
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: Gunma University
• Principal Investigator: Terawaki Shin-ichi 群馬大学, 大学院理工学府, 助教 (10452533)
• Project Period (FY): 2013-04-01 – 2017-03-31
• 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

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.

Free Research Field

構造生物化学