Expression, crystallization and preliminary X-ray studies of the PDZ domain of Dishevelled protein

Acta Crystallogr D Biol Crystallogr. 2000 Feb;56(Pt 2):212-4. doi: 10.1107/s0907444999016054.

Abstract

Dishevelled (Dsh) protein is an important component of the Wnt signal-transduction pathway. It has three relatively conserved domains: DIX, PDZ and DEP. The PDZ domain of the Xenopus laevis homolog of Dsh, which consists of residues 254-348, was overexpressed as a soluble protein in Escherichia coli, purified and crystallized. The crystals were obtained by the vapor-diffusion method, using 1.4 M sodium formate as a precipitant. The crystals diffracted to 2.3 A resolution. The space group was determined to be P6(1)22 or P6(5)22, with unit-cell dimensions a = b = 95.9, c = 93.9 A.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • Crystallization
  • Crystallography, X-Ray
  • Dishevelled Proteins
  • Escherichia coli / chemistry
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Phosphoproteins / biosynthesis
  • Phosphoproteins / chemistry*
  • Phosphoproteins / genetics
  • Phosphoproteins / isolation & purification
  • Protein Structure, Tertiary
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / isolation & purification
  • Xenopus Proteins
  • Xenopus laevis

Substances

  • Adaptor Proteins, Signal Transducing
  • DVL1 protein, Xenopus
  • Dishevelled Proteins
  • Phosphoproteins
  • Recombinant Proteins
  • Xenopus Proteins