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| | ==Crystal structure of human BMP9 at 1.87 A resolution== | | ==Crystal structure of human BMP9 at 1.87 A resolution== |
| - | <StructureSection load='5i05' size='340' side='right' caption='[[5i05]], [[Resolution|resolution]] 1.87Å' scene=''> | + | <StructureSection load='5i05' size='340' side='right'caption='[[5i05]], [[Resolution|resolution]] 1.87Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5i05]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I05 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I05 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5i05]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I05 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5I05 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.87Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5i04|5i04]], [[5hzw|5hzw]], [[5hzv|5hzv]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5i05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i05 OCA], [http://pdbe.org/5i05 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i05 RCSB], [http://www.ebi.ac.uk/pdbsum/5i05 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i05 ProSAT]</span></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=5i05 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i05 OCA], [https://pdbe.org/5i05 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5i05 RCSB], [https://www.ebi.ac.uk/pdbsum/5i05 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5i05 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[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> | + | [https://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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5i05" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5i05" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Growth differentiation factor 3D STRUCTURES|Growth differentiation factor 3D STRUCTURES]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bokhove, M]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Jovine, L]] | + | [[Category: Large Structures]] |
| - | [[Category: Saito, T]] | + | [[Category: Bokhove M]] |
| - | [[Category: Angiogenesis]] | + | [[Category: Jovine L]] |
| - | [[Category: Cell proliferation signal]] | + | [[Category: Saito T]] |
| - | [[Category: Cytokine]]
| + | |
| - | [[Category: Growth differentiation factor 2]]
| + | |
| - | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
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.[1] [2]
Publication Abstract from PubMed
Endoglin (ENG)/CD105 is an essential endothelial cell co-receptor of the transforming growth factor beta (TGF-beta) superfamily, mutated in hereditary hemorrhagic telangiectasia type 1 (HHT1) and involved in tumor angiogenesis and preeclampsia. Here, we present crystal structures of the ectodomain of human ENG and its complex with the ligand bone morphogenetic protein 9 (BMP9). BMP9 interacts with a hydrophobic surface of the N-terminal orphan domain of ENG, which adopts a new duplicated fold generated by circular permutation. The interface involves residues mutated in HHT1 and overlaps with the epitope of tumor-suppressing anti-ENG monoclonal TRC105. The structure of the C-terminal zona pellucida module suggests how two copies of ENG embrace homodimeric BMP9, whose binding is compatible with ligand recognition by type I but not type II receptors. These findings shed light on the molecular basis of the BMP signaling cascade, with implications for future therapeutic interventions in this fundamental pathway.
Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1.,Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L Cell Rep. 2017 May 30;19(9):1917-1928. doi: 10.1016/j.celrep.2017.05.011. PMID:28564608[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ David L, Mallet C, Keramidas M, Lamande N, Gasc JM, Dupuis-Girod S, Plauchu H, Feige JJ, Bailly S. Bone morphogenetic protein-9 is a circulating vascular quiescence factor. Circ Res. 2008 Apr 25;102(8):914-22. doi: 10.1161/CIRCRESAHA.107.165530. Epub, 2008 Feb 28. PMID:18309101 doi:10.1161/CIRCRESAHA.107.165530
- ↑ Mahlawat P, Ilangovan U, Biswas T, Sun LZ, Hinck AP. Structure of the Alk1 extracellular domain and characterization of its bone morphogenetic protein (BMP) binding properties. Biochemistry. 2012 Aug 14;51(32):6328-41. Epub 2012 Aug 2. PMID:22799562 doi:10.1021/bi300942x
- ↑ Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L. Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1. Cell Rep. 2017 May 30;19(9):1917-1928. doi: 10.1016/j.celrep.2017.05.011. PMID:28564608 doi:http://dx.doi.org/10.1016/j.celrep.2017.05.011
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