Purification, crystallization and preliminary data analysis of the ligand-receptor complex of the growth and differentiation factor 5 variant R57A (GDF5R57A) and BMP receptor IA (BRIA)

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):551-5. doi: 10.1107/S1744309111006907. Epub 2011 Apr 21.

Abstract

The binary ligand-receptor complex of human growth and differentiation factor 5 (GDF5) bound to its type I receptor BMP receptor IA (BRIA) was prepared and crystallized. By utilizing the GDF5 variant R57A, which exhibits a high affinity in the subnanomolar range for BRIA, the binary complex of GDF5R57A bound to the extracellular domain of BRIA could be produced and purified. Crystals of this complex belonged to a monoclinic space group: either I2, with unit-cell parameters a = 63.81, b = 62.85, c = 124.99 Å, β = 95.9°, or C2, with unit-cell parameters a = 132.17, b = 62.78, c = 63.53 Å, β = 112.8°.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bone Morphogenetic Protein Receptors, Type I / chemistry*
  • Bone Morphogenetic Protein Receptors, Type I / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Growth Differentiation Factor 5 / chemistry*
  • Growth Differentiation Factor 5 / genetics
  • Growth Differentiation Factor 5 / isolation & purification
  • Humans
  • Ligands
  • Mutation
  • Protein Binding

Substances

  • GDF5 protein, human
  • Growth Differentiation Factor 5
  • Ligands
  • Bone Morphogenetic Protein Receptors, Type I