4yci | pdb_00004yci

non-latent pro-bone morphogenetic protein 9

spinqualitylabelsall models 4yci, resolution 3.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yci is a 4 chain structure with sequence from Homo sapiens and Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Growth differentiation factor 3D STRUCTURES

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