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4dou
From Proteopedia
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| - | [[ | + | ==Crystal Structure of a Single-chain Trimer of Human Adiponectin Globular Domain== |
| + | <StructureSection load='4dou' size='340' side='right' caption='[[4dou]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4dou]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4DOU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4DOU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1c28|1c28]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ACDC, ACRP30, adiponectin, ADIPOQ, APM1, GBP28 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4dou FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4dou OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4dou RCSB], [http://www.ebi.ac.uk/pdbsum/4dou PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/RBTN2_MOUSE RBTN2_MOUSE]] Acts with TAL1/SCL to regulate red blood cell development. Also acts with LDB1 to maintain erythroid precursors in an immature state.<ref>PMID:9391090</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Adiponectin is increasingly recognized as a potential therapeutic agent for the treatment of diabetes and other metabolic diseases. It circulates in plasma as homotrimers and higher-order oliogomers of homotrimers. To facilitate the production of active recombinant adiponectin as a therapeutic tool, we designed a single-chain globular domain adiponectin (sc-gAd) in which three monomer sequences are linked together in tandem to form one contiguous polypeptide. Here, we present the crystal structure of human sc-gAd at 2.0A resolution. The structure reveals a similar trimeric topology to that of mouse gAd protein. Trimer formation is further rigidified by three calcium ions. | ||
| - | + | Crystal structure of a single-chain trimer of human adiponectin globular domain.,Min X, Lemon B, Tang J, Liu Q, Zhang R, Walker N, Li Y, Wang Z FEBS Lett. 2012 Mar 23;586(6):912-7. Epub 2012 Feb 22. PMID:22449980<ref>PMID:22449980</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
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| - | == | + | |
| - | < | + | |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Min, X | + | [[Category: Min, X]] |
| - | [[Category: Walker, N P | + | [[Category: Walker, N P]] |
| - | [[Category: Wang, Z | + | [[Category: Wang, Z]] |
[[Category: C1q-like domain]] | [[Category: C1q-like domain]] | ||
[[Category: Calcium binding]] | [[Category: Calcium binding]] | ||
Revision as of 06:52, 25 December 2014
Crystal Structure of a Single-chain Trimer of Human Adiponectin Globular Domain
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