4ycg
From Proteopedia
(Difference between revisions)
| Line 8: | Line 8: | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/GDF2_MOUSE GDF2_MOUSE]] Potent circulating inhibitor of angiogenesis. Could be involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG.<ref>PMID:23300529</ref> [[http://www.uniprot.org/uniprot/GDF2_HUMAN GDF2_HUMAN]] Potent circulating inhibitor of angiogenesis. Could be involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks.<ref>PMID:18309101</ref> <ref>PMID:22799562</ref> | [[http://www.uniprot.org/uniprot/GDF2_MOUSE GDF2_MOUSE]] Potent circulating inhibitor of angiogenesis. Could be involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks. Signaling through SMAD1 in endothelial cells requires TGF-beta coreceptor endoglin/ENG.<ref>PMID:23300529</ref> [[http://www.uniprot.org/uniprot/GDF2_HUMAN GDF2_HUMAN]] Potent circulating inhibitor of angiogenesis. Could be involved in bone formation. Signals through the type I activin receptor ACVRL1 but not other Alks.<ref>PMID:18309101</ref> <ref>PMID:22799562</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bone morphogenetic proteins (BMPs) belong to the TGF-beta family, whose 33 members regulate multiple aspects of morphogenesis. TGF-beta family members are secreted as procomplexes containing a small growth factor dimer associated with two larger prodomains. As isolated procomplexes, some members are latent, whereas most are active; what determines these differences is unknown. Here, studies on pro-BMP structures and binding to receptors lead to insights into mechanisms that regulate latency in the TGF-beta family and into the functions of their highly divergent prodomains. The observed open-armed, nonlatent conformation of pro-BMP9 and pro-BMP7 contrasts with the cross-armed, latent conformation of pro-TGF-beta1. Despite markedly different arm orientations in pro-BMP and pro-TGF-beta, the arm domain of the prodomain can similarly associate with the growth factor, whereas prodomain elements N- and C-terminal to the arm associate differently with the growth factor and may compete with one another to regulate latency and stepwise displacement by type I and II receptors. Sequence conservation suggests that pro-BMP9 can adopt both cross-armed and open-armed conformations. We propose that interactors in the matrix stabilize a cross-armed pro-BMP conformation and regulate transition between cross-armed, latent and open-armed, nonlatent pro-BMP conformations. | ||
| + | |||
| + | Structure of bone morphogenetic protein 9 procomplex.,Mi LZ, Brown CT, Gao Y, Tian Y, Le VQ, Walz T, Springer TA Proc Natl Acad Sci U S A. 2015 Mar 24;112(12):3710-5. doi:, 10.1073/pnas.1501303112. Epub 2015 Mar 6. PMID:25751889<ref>PMID:25751889</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 07:50, 26 March 2015
Pro-bone morphogenetic protein 9
| |||||||||||
