Isolation of recombinant BMP receptor IA ectodomain and its 2 : 1 complex with BMP-2

Citation
T. Kirsch et al., Isolation of recombinant BMP receptor IA ectodomain and its 2 : 1 complex with BMP-2, FEBS LETTER, 468(2-3), 2000, pp. 215-219
Citations number
36
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
468
Issue
2-3
Year of publication
2000
Pages
215 - 219
Database
ISI
SICI code
0014-5793(20000225)468:2-3<215:IORBRI>2.0.ZU;2-K
Abstract
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 olig omerization of type I and type II serine/threonine kinase receptors, We rep ort here expression of the extracellular domain of the human type IA recept or for BMP-2 (BMPR-IA) in Escherichia coli. This soluble form of BMPR-IA (s BMPR-IA) was purified employing a BMP-2 affinity column, Cel filtration exp eriments and analysis of gel filtration fractions by polyacrylamide electro phoresis and densitometry reveal that BMP-2 forms a defined 1:2 complex wit h sBMPR-IA. that can be purified and hopefully used for crystallization stu dies. (C) 2000 Federation of European Biochemical Societies.