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3hh2
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HH2 FirstGlance]. <br> | <table><tr><td colspan='2'>[[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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3HH2 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CIT:CITRIC+ACID'>CIT</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr><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=10090 Mus musculus]), FST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=10090 Mus musculus]), FST ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3hh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hh2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hh2 RCSB], [http://www.ebi.ac.uk/pdbsum/3hh2 PDBsum]</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=3hh2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hh2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3hh2 RCSB], [http://www.ebi.ac.uk/pdbsum/3hh2 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/GDF8_MOUSE GDF8_MOUSE]] Acts specifically as a negative regulator of skeletal muscle growth. [[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). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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> | 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> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Group:MUZIC:Myostatin|MUZIC:Myostatin]] | ||
| + | *[[Growth differentiation factor|Growth differentiation factor]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
| - | [[Category: Cash, J N | + | [[Category: Cash, J N]] |
| - | [[Category: Thompson, T B | + | [[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]] | ||
Revision as of 07:20, 25 December 2014
Crystal structure of the myostatin:follistatin 288 complex
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Categories: Homo sapiens | Mus musculus | Cash, J N | Thompson, T B | Cleavage on pair of basic residue | Cystine knot motif | Cytokine | Disulfide bond | Disulfide linked dimer | Glycoprotein | Growth factor | Protein-protein complex | Secreted | Signaling protein-cytokine complex | Tb domain | Tgf-beta fold
