Purification, crystallization and preliminary data analysis of ligand–receptor complexes of growth and differentiation factor 5 (GDF5) and BMP receptor IB (BRIB)
| Autor: | Joachim Nickel, Thomas D. Mueller, Alexander Kotzsch, Walter Sebald |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Protein Conformation education Biophysics Crystallography X-Ray Ligands Biochemistry law.invention Mice Tetragonal crystal system Protein structure Growth Differentiation Factor 5 Structural Biology law Genetics Extracellular Animals Humans Crystallization Receptor Ternary complex Bone Morphogenetic Protein Receptors Type I Chemistry Ligand Condensed Matter Physics Recombinant Proteins Crystallography Crystallization Communications Recombinant DNA Electrophoresis Polyacrylamide Gel |
| Zdroj: | Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65:779-783 |
| ISSN: | 1744-3091 |
| DOI: | 10.1107/s1744309109024142 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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