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| | <StructureSection load='5jhw' size='340' side='right'caption='[[5jhw]], [[Resolution|resolution]] 2.35Å' scene=''> | | <StructureSection load='5jhw' size='340' side='right'caption='[[5jhw]], [[Resolution|resolution]] 2.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jhw]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JHW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jhw]] is a 4 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=5JHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JHW FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</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]] 2.35Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5ji1|5ji1]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GDF11, BMP11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), FST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=5jhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhw OCA], [https://pdbe.org/5jhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jhw RCSB], [https://www.ebi.ac.uk/pdbsum/5jhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhw ProSAT]</span></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=5jhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhw OCA], [http://pdbe.org/5jhw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jhw RCSB], [http://www.ebi.ac.uk/pdbsum/5jhw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/GDF11_HUMAN GDF11_HUMAN]] Secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development. Play critical roles in patterning both mesodermal and neural tissues and in establishing the skeletal pattern. [[http://www.uniprot.org/uniprot/FST_HUMAN FST_HUMAN]] Binds directly to activin and functions as an activin antagonist. Specific inhibitor of the biosynthesis and secretion of pituitary follicle stimulating hormone (FSH). | + | [https://www.uniprot.org/uniprot/GDF11_HUMAN GDF11_HUMAN] Secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development. Play critical roles in patterning both mesodermal and neural tissues and in establishing the skeletal pattern. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | | | |
| | ==See Also== | | ==See Also== |
| | + | *[[Follistatin|Follistatin]] |
| | *[[Growth differentiation factor 3D STRUCTURES|Growth differentiation factor 3D STRUCTURES]] | | *[[Growth differentiation factor 3D STRUCTURES|Growth differentiation factor 3D STRUCTURES]] |
| | == References == | | == References == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Thompson, T B]] | + | [[Category: Thompson TB]] |
| - | [[Category: Walker, R G]] | + | [[Category: Walker RG]] |
| - | [[Category: Cytokine-signaling protein complex]]
| + | |
| - | [[Category: Follistatin]]
| + | |
| - | [[Category: Gdf11]]
| + | |
| - | [[Category: Ligand]]
| + | |
| - | [[Category: Tgfbeta]]
| + | |
| Structural highlights
Function
GDF11_HUMAN Secreted signal that acts globally to specify positional identity along the anterior/posterior axis during development. Play critical roles in patterning both mesodermal and neural tissues and in establishing the skeletal pattern.
Publication Abstract from PubMed
BACKGROUND: Growth/differentiation factor 8 (GDF8) and GDF11 are two highly similar members of the transforming growth factor beta (TGFbeta) family. While GDF8 has been recognized as a negative regulator of muscle growth and differentiation, there are conflicting studies on the function of GDF11 and whether GDF11 has beneficial effects on age-related dysfunction. To address whether GDF8 and GDF11 are functionally identical, we compared their signaling and structural properties. RESULTS: Here we show that, despite their high similarity, GDF11 is a more potent activator of SMAD2/3 and signals more effectively through the type I activin-like receptor kinase receptors ALK4/5/7 than GDF8. Resolution of the GDF11:FS288 complex, apo-GDF8, and apo-GDF11 crystal structures reveals unique properties of both ligands, specifically in the type I receptor binding site. Lastly, substitution of GDF11 residues into GDF8 confers enhanced activity to GDF8. CONCLUSIONS: These studies identify distinctive structural features of GDF11 that enhance its potency, relative to GDF8; however, the biological consequences of these differences remain to be determined.
Structural basis for potency differences between GDF8 and GDF11.,Walker RG, Czepnik M, Goebel EJ, McCoy JC, Vujic A, Cho M, Oh J, Aykul S, Walton KL, Schang G, Bernard DJ, Hinck AP, Harrison CA, Martinez-Hackert E, Wagers AJ, Lee RT, Thompson TB BMC Biol. 2017 Mar 3;15(1):19. doi: 10.1186/s12915-017-0350-1. PMID:28257634[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Walker RG, Czepnik M, Goebel EJ, McCoy JC, Vujic A, Cho M, Oh J, Aykul S, Walton KL, Schang G, Bernard DJ, Hinck AP, Harrison CA, Martinez-Hackert E, Wagers AJ, Lee RT, Thompson TB. Structural basis for potency differences between GDF8 and GDF11. BMC Biol. 2017 Mar 3;15(1):19. doi: 10.1186/s12915-017-0350-1. PMID:28257634 doi:http://dx.doi.org/10.1186/s12915-017-0350-1
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