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Title
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Isolation of recombinant BMP receptor IA ectodomain and its 2:1 complex with BMP-2.
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Authors
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T.Kirsch,
J.Nickel,
W.Sebald.
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Ref.
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Febs Lett, 2000,
468,
215-219.
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PubMed id
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Abstract
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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.
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