5ntu: Difference between revisions

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 <StructureSection load='5ntu' size='340' side='right' caption='[[5ntu]], [[Resolution|resolution]] 2.58&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5ntu]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NTU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5ntu]] 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=5NTU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NTU FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=5ntu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ntu OCA], [http://pdbe.org/5ntu PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ntu RCSB], [http://www.ebi.ac.uk/pdbsum/5ntu PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ntu ProSAT]</span></td></tr>
 </table>
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 == Function ==
 [[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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 5ntu" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Cotton, T R]]
 [[Category: Fischer, G]]