1lxi
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(New page: 200px<br /> <applet load="1lxi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lxi, resolution 2.00Å" /> '''Refinement of BMP7 ...)
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Revision as of 15:58, 12 November 2007
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Refinement of BMP7 crystal structure
Overview
Activins and bone morphogenetic proteins (BMPs) elicit diverse biological, responses by signaling through two pairs of structurally related type I, and type II receptors. Here we report the crystal structure of BMP7 in, complex with the extracellular domain (ECD) of the activin type II, receptor. Our structure produces a compelling four-receptor model, revealing that the types I and II receptor ECDs make no direct contacts., Nevertheless, we find that truncated receptors lacking their cytoplasmic, domain retain the ability to cooperatively assemble in the cell membrane., Also, the affinity of BMP7 for its low-affinity type I receptor ECD, increases 5-fold in the presence of its type II receptor ECD. Taken, together, our results provide a view of the ligand-mediated cooperative, assembly of BMP and activin receptors that does not rely on, receptor-receptor contacts.
About this Structure
1LXI is a Single protein structure of sequence from Homo sapiens with NAG as ligand. Full crystallographic information is available from OCA.
Reference
The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly., Greenwald J, Groppe J, Gray P, Wiater E, Kwiatkowski W, Vale W, Choe S, Mol Cell. 2003 Mar;11(3):605-17. PMID:12667445
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