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    FEBS Lett. 2000 Feb 25;468(2-3):215-9.

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

    Kirsch T, Nickel J, Sebald W.

    Source

    Physiologische Chemie II, Biozentrum der Universität Würzburg, Am Hubland, D-97074, Würzburg, Germany. kirsch@biozentrum.uni-wuerzburg.de

    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 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.

    PMID:
    10692589
    [PubMed - indexed for MEDLINE]

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