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5nxs
From Proteopedia
(Difference between revisions)
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<StructureSection load='5nxs' size='340' side='right' caption='[[5nxs]], [[Resolution|resolution]] 4.19Å' scene=''> | <StructureSection load='5nxs' size='340' side='right' caption='[[5nxs]], [[Resolution|resolution]] 4.19Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[5nxs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NXS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NXS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5nxs]] is a 2 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=5NXS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NXS FirstGlance]. <br> |
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MSTN, GDF8 ([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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5nxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxs OCA], [http://pdbe.org/5nxs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nxs RCSB], [http://www.ebi.ac.uk/pdbsum/5nxs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxs 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=5nxs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5nxs OCA], [http://pdbe.org/5nxs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5nxs RCSB], [http://www.ebi.ac.uk/pdbsum/5nxs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5nxs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/GDF8_HUMAN GDF8_HUMAN]] Acts specifically as a negative regulator of skeletal muscle growth. | [[http://www.uniprot.org/uniprot/GDF8_HUMAN GDF8_HUMAN]] Acts specifically as a negative regulator of skeletal muscle growth. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Myostatin, a key regulator of muscle mass in vertebrates, is biosynthesised as a latent precursor in muscle and is activated by sequential proteolysis of the pro-domain. To investigate the molecular mechanism by which pro-myostatin remains latent, we have determined the structure of unprocessed pro-myostatin and analysed the properties of the protein in its different forms. Crystal structures and SAXS analyses show that pro-myostatin adopts an open, V-shaped structure with a domain-swapped arrangement. The pro-mature complex, after cleavage of the furin site, has significantly reduced activity compared with the mature growth factor and persists as a stable complex that is resistant to the natural antagonist follistatin. The latency appears to be conferred by a number of distinct features that collectively stabilise the interaction of the pro-domains with the mature growth factor, enabling a regulated stepwise activation process, distinct from the prototypical pro-TGF-beta1. These results provide a basis for understanding the effect of missense mutations in pro-myostatin and pave the way for the design of novel myostatin inhibitors. | ||
| + | |||
| + | Structure of the human myostatin precursor and determinants of growth factor latency.,Cotton TR, Fischer G, Wang X, McCoy JC, Czepnik M, Thompson TB, Hyvonen M EMBO J. 2018 Jan 12. pii: embj.201797883. doi: 10.15252/embj.201797883. PMID:29330193<ref>PMID:29330193</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5nxs" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Human]] | ||
[[Category: Cotton, T R]] | [[Category: Cotton, T R]] | ||
[[Category: Fischer, G]] | [[Category: Fischer, G]] | ||
Revision as of 20:43, 24 January 2018
Crystal Structure of Human Pro-myostatin Precursor at 4.2 A Resolution with Experimental Phases from SeMet labelling
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