Open AccessCrystallographic characterization of the DIX domain of the Wnt signalling positive regulator Ccd1
Author(s) -
Terawaki Shinichi,
Yano Koumei,
Katsutani Takuya,
Shiomi Kensuke,
KeinoMasu Kazuko,
Masu Masayuki,
Shomura Yasuhito,
Komori Hirofumi,
Shibata Naoki,
Higuchi Yoshiki
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111016526
Subject(s) - regulator , characterization (materials science) , domain (mathematical analysis) , signalling , microbiology and biotechnology , chemistry , wnt signaling pathway , computational biology , materials science , biology , nanotechnology , biochemistry , mathematics , signal transduction , gene , mathematical analysis
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 domain are reported. The crystals of the Ccd1 DIX domain belonged to space group P 2 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.