Purification, crystallization and preliminary data analysis of ligand-receptor complexes of growth and differentiation factor 5 (GDF5) and BMP receptor IB (BRIB)

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Aug 1;65(Pt 8):779-83. doi: 10.1107/S1744309109024142. Epub 2009 Jul 25.

Abstract

The ligand-receptor complex of GDF5 bound to its type I and type II receptors BRIB and ActRIIB was produced and crystallized. Crystals of the GDF5-BRIB complex could only be obtained if a ternary complex comprising GDF5, BRIB and the extracellular domain of the type II receptor ActRIIB was used in crystallization; however, the type II receptor ActRIIB was lost during crystallization. Crystals of this complex belonged to the tetragonal space group P4(2)2(1)2, with unit-cell parameters a = b = 76.46, c = 82.78 A. Small changes in the crystallization condition resulted in crystals with a different morphology. These crystals consisted of the full ternary complex GDF5-BRIB-ActRIIB, but only diffracted to low resolution.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Bone Morphogenetic Protein Receptors, Type I / chemistry*
  • Bone Morphogenetic Protein Receptors, Type I / isolation & purification
  • Crystallization
  • Crystallography, X-Ray
  • Electrophoresis, Polyacrylamide Gel
  • Growth Differentiation Factor 5 / chemistry*
  • Growth Differentiation Factor 5 / isolation & purification
  • Humans
  • Ligands
  • Mice
  • Models, Molecular
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification

Substances

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