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1lx5
From Proteopedia
Crystal Structure of the BMP7/ActRII Extracellular Domain Complex
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1LX5 is a 2 chains structure of sequences from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA.
Reference
- Greenwald J, Groppe J, Gray P, Wiater E, Kwiatkowski W, Vale W, Choe S. The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly. Mol Cell. 2003 Mar;11(3):605-17. PMID:12667445
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