Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2.
Bone morphogenetic protein-2 (BMP-2) is a member of the transforming growth factor beta superfamily which induces bone formation and regeneration, and important steps during early embryonic development. BMP-2 signals via oligomerization of type I and type II serine/threonine kinase receptors. We report here expression of the extracellular domain of the ... human type IA receptor for BMP-2 (BMPR-IA) in Escherichia coli. This soluble form of BMPR-IA (sBMPR-IA) was purified employing a BMP-2 affinity column. Gel filtration experiments and analysis of gel filtration fractions by polyacrylamide electrophoresis and densitometry reveal that BMP-2 forms a defined 1:2 complex with sBMPR-IA that can be purified and hopefully used for crystallization studies.
Mesh Terms:
Binding Sites, Bone Morphogenetic Protein 2, Bone Morphogenetic Protein Receptors, Type I, Bone Morphogenetic Proteins, Chromatography, Gel, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Humans, Kinetics, Protein-Serine-Threonine Kinases, Receptors, Growth Factor, Recombinant Proteins, Transforming Growth Factor beta
Binding Sites, Bone Morphogenetic Protein 2, Bone Morphogenetic Protein Receptors, Type I, Bone Morphogenetic Proteins, Chromatography, Gel, Cloning, Molecular, Electrophoresis, Polyacrylamide Gel, Escherichia coli, Humans, Kinetics, Protein-Serine-Threonine Kinases, Receptors, Growth Factor, Recombinant Proteins, Transforming Growth Factor beta
FEBS Lett.
Date: Feb. 25, 2000
PubMed ID: 10692589
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