View source for 4ycg


==Pro-bone morphogenetic protein 9==
<StructureSection load='4ycg' size='340' side='right'caption='[[4ycg]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4ycg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YCG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YCG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4ycg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ycg OCA], [https://pdbe.org/4ycg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ycg RCSB], [https://www.ebi.ac.uk/pdbsum/4ycg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ycg ProSAT]</span></td></tr>
</table>
== Function ==
[https://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> 
<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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4ycg" style="background-color:#fffaf0;"></div>

==See Also==
*[[Growth differentiation factor 3D STRUCTURES|Growth differentiation factor 3D STRUCTURES]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Brown CT]]
[[Category: Gao Y]]
[[Category: Le V]]
[[Category: Mi L-Z]]
[[Category: Springer TA]]
[[Category: Tian Y]]
[[Category: Walz T]]