Purification, crystallization and preliminary data analysis of ligand-receptor complexes of growth and differentiation factor 5 (GDF5) and BMP receptor IB (BRIB).
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.
Kotzsch
Alexander
A
Lehrstuhl für Botanik I - Molekulare Pflanzenphysiologie und Biophysik, Julius-von-Sachs-Institut für Biowissenschaften (Biozentrum) der Universität Würzburg, Julius-von-Sachs-Platz 2, D-97082 Würzburg, Germany.
Nickel
Joachim
J
Sebald
Walter
W
Mueller
Thomas D
TD
D000818:Animals; D052005:Bone Morphogenetic Protein Receptors, Type I / Q000737:chemistry* / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D055428:Growth Differentiation Factor 5 / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans; D008024:Ligands; D051379:Mice; D008958:Models, Molecular; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification
C525893:GDF5 protein, human; D055428:Growth Differentiation Factor 5; D008024:Ligands; D011994:Recombinant Proteins; D052005:Bone Morphogenetic Protein Receptors, Type I