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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Jul 1;67(Pt 7):758-61. doi: 10.1107/S1744309111016526. Epub 2011 Jun 30.

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 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 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallography, X-Ray
  • Intracellular Signaling Peptides and Proteins / chemistry*
  • Intracellular Signaling Peptides and Proteins / metabolism
  • Mice
  • Signal Transduction*
  • Wnt Proteins / metabolism

Substances

  • Dixdc1 protein, mouse
  • Intracellular Signaling Peptides and Proteins
  • Wnt Proteins