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3hh2

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[[Image:3hh2.png|left|200px]]
 
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==Crystal structure of the myostatin:follistatin 288 complex==
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The line below this paragraph, containing "STRUCTURE_3hh2", creates the "Structure Box" on the page.
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<StructureSection load='3hh2' size='340' side='right'caption='[[3hh2]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3hh2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human] and [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HH2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HH2 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Mstn, Gdf8 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), FST ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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{{STRUCTURE_3hh2| PDB=3hh2 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hh2 OCA], [https://pdbe.org/3hh2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hh2 RCSB], [https://www.ebi.ac.uk/pdbsum/3hh2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hh2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/GDF8_MOUSE GDF8_MOUSE]] Acts specifically as a negative regulator of skeletal muscle growth. [[https://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).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hh/3hh2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3hh2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Myostatin is a member of the transforming growth factor-beta (TGF-beta) family and a strong negative regulator of muscle growth. Here, we present the crystal structure of myostatin in complex with the antagonist follistatin 288 (Fst288). We find that the prehelix region of myostatin very closely resembles that of TGF-beta class members and that this region alone can be swapped into activin A to confer signalling through the non-canonical type I receptor Alk5. Furthermore, the N-terminal domain of Fst288 undergoes conformational rearrangements to bind myostatin and likely acts as a site of specificity for the antagonist. In addition, a unique continuous electropositive surface is created when myostatin binds Fst288, which significantly increases the affinity for heparin. This translates into stronger interactions with the cell surface and enhanced myostatin degradation in the presence of either Fst288 or Fst315. Overall, we have identified several characteristics unique to myostatin that will be paramount to the rational design of myostatin inhibitors that could be used in the treatment of muscle-wasting disorders.
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===Crystal structure of the myostatin:follistatin 288 complex===
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The structure of myostatin:follistatin 288: insights into receptor utilization and heparin binding.,Cash JN, Rejon CA, McPherron AC, Bernard DJ, Thompson TB EMBO J. 2009 Sep 2;28(17):2662-76. Epub 2009 Jul 30. PMID:19644449<ref>PMID:19644449</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3hh2" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 19644449 is the PubMed ID number.
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{{ABSTRACT_PUBMED_19644449}}
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==About this Structure==
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[[3hh2]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HH2 OCA].
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==See Also==
==See Also==
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*[[Group:MUZIC:Myostatin]]
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*[[Follistatin|Follistatin]]
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*[[Growth differentiation factor 3D STRUCTURES|Growth differentiation factor 3D STRUCTURES]]
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==Reference==
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== References ==
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<ref group="xtra">PMID:019644449</ref><references group="xtra"/>
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<references/>
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[[Category: Homo sapiens]]
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__TOC__
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[[Category: Mus musculus]]
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</StructureSection>
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[[Category: Cash, J N.]]
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[[Category: Human]]
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[[Category: Thompson, T B.]]
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[[Category: Large Structures]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Cash, J N]]
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[[Category: Thompson, T B]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Cystine knot motif]]
[[Category: Cystine knot motif]]
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[[Category: Tb domain]]
[[Category: Tb domain]]
[[Category: Tgf-beta fold]]
[[Category: Tgf-beta fold]]
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[[Category: Z-disk]]

Current revision

Crystal structure of the myostatin:follistatin 288 complex

PDB ID 3hh2

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OCA

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