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Crystallographic characterization of the DIX domain of the Wnt signalling positive regulator Ccd1.

ABSTRACT: Coiled-coil DIX1 (Ccd1) is a positive regulator that activates the canonical Wnt signalling pathway by inhibiting the degradation of the key signal transducer ?-catenin. The C-terminal DIX domain of Ccd1 plays an important role in the regulation of signal transduction through homo-oligomerization and protein complex formation with other DIX domain-containing proteins, i.e. axin and dishevelled proteins. Here, the expression, purification, crystallization and X-ray data collection of the Ccd1 DIX domain are reported. The crystals of the Ccd1 DIX domain belonged to space group P2(1)2(1)2(1), with unit-cell parameters a=72.9, b=75.7, c=125.6?Å. An X-ray diffraction data set was collected at 3.0?Å resolution.

SUBMITTER: Terawaki S

PROVIDER: S-EPMC3144790 | biostudies-literature | 2011 Jul

REPOSITORIES: biostudies-literature

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Crystallographic characterization of the DIX domain of the Wnt signalling positive regulator Ccd1.

Terawaki Shin-ichi S Yano Koumei K Katsutani Takuya T Shiomi Kensuke K Keino-Masu Kazuko K Masu Masayuki M Shomura Yasuhito Y Komori Hirofumi H Shibata Naoki N Higuchi Yoshiki Y

Acta crystallographica. Section F, Structural biology and crystallization communications 20110630 Pt 7

Coiled-coil DIX1 (Ccd1) is a positive regulator that activates the canonical Wnt signalling pathway by inhibiting the degradation of the key signal transducer β-catenin. The C-terminal DIX domain of Ccd1 plays an important role in the regulation of signal transduction through homo-oligomerization and protein complex formation with other DIX domain-containing proteins, i.e. axin and dishevelled proteins. Here, the expression, purification, crystallization and X-ray data collection of the Ccd1 DIX ...[more]

PMID: 21795788

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Molecular basis of Wnt activation via the DIX domain protein Ccd1.

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