4mac
From Proteopedia
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| - | ''' | + | ==Crystal structure of CIDE-N domain of FSP27== |
| + | <StructureSection load='4mac' size='340' side='right' caption='[[4mac]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4mac]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MAC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MAC FirstGlance]. <br> | ||
| + | </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=4mac FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mac OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mac RCSB], [http://www.ebi.ac.uk/pdbsum/4mac PDBsum]</span></td></tr> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | FSP27 (CIDE-3 in humans) plays critical roles in lipid metabolism and apoptosis and is known to be involved in regulation of lipid droplet (LD) size and lipid storage and apoptotic DNA fragmentation. Given that CIDE-containing proteins including FSP27 are associated with many human diseases including cancer, aging, diabetes, and obesity, studies of FSP27 and other CIDE-containing proteins are of great biological importance. As a first step toward elucidating the molecular mechanisms of FSP27-mediated lipid droplet growth and apoptosis, we report the crystal structure of the CIDE-N domain of FSP27 at a resolution of 2.0 A. The structure revealed a possible biologically important homo-dimeric interface similar to that formed by the hetero-dimeric complex, CAD/ICAD. Comparison with other structural homologues revealed that the PB1 domain of BEM1P, ubiquitin-like domain of BAG6 and ubiquitin are structurally similar proteins. Our homo-dimeric structure of the CIDE-N domain of FSP27 will provide important information that will enable better understanding of the function of FSP27. | ||
| - | + | Molecular basis for homo-dimerization of the CIDE domain revealed by the crystal structure of the CIDE-N domain of FSP27.,Lee SM, Jang TH, Park HH Biochem Biophys Res Commun. 2013 Oct 4;439(4):564-9. doi:, 10.1016/j.bbrc.2013.09.018. Epub 2013 Sep 8. PMID:24025675<ref>PMID:24025675</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Lee, S M.]] | ||
| + | [[Category: Park, H H.]] | ||
| + | [[Category: Apoptosis]] | ||
| + | [[Category: Perilipin1]] | ||
| + | [[Category: Protein interaction]] | ||
| + | [[Category: Roll fold]] | ||
Revision as of 08:21, 2 July 2014
Crystal structure of CIDE-N domain of FSP27
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