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| | <StructureSection load='5xpc' size='340' side='right'caption='[[5xpc]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='5xpc' size='340' side='right'caption='[[5xpc]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5xpc]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XPC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5XPC FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5xpc]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XPC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XPC FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.902Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Drep4, Drep-4, drep4, Rep4, CG9414, Dmel_CG9414 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=5xpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xpc OCA], [http://pdbe.org/5xpc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5xpc RCSB], [http://www.ebi.ac.uk/pdbsum/5xpc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5xpc ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5xpc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xpc OCA], [https://pdbe.org/5xpc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xpc RCSB], [https://www.ebi.ac.uk/pdbsum/5xpc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xpc ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q9V3H0_DROME Q9V3H0_DROME] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Jeong, J H]] | + | [[Category: Jeong JH]] |
| - | [[Category: Park, H H]] | + | [[Category: Park HH]] |
| - | [[Category: Apoptosis]]
| + | |
| - | [[Category: Cide]]
| + | |
| - | [[Category: Dna fragmentation factor]]
| + | |
| - | [[Category: Drep4]]
| + | |
| - | [[Category: Energy metabolism]]
| + | |
| Structural highlights
Function
Q9V3H0_DROME
Publication Abstract from PubMed
Cell death-inducing DFF45-like effector (CIDE) domains, initially identified in apoptotic nucleases, form a family with diverse functions ranging from cell death to lipid homeostasis. Here we show that the CIDE domains of Drosophila and human apoptotic nucleases Drep2, Drep4, and DFF40 all form head-to-tail helical filaments. Opposing positively and negatively charged interfaces mediate the helical structures, and mutations on these surfaces abolish nuclease activation for apoptotic DNA fragmentation. Conserved filamentous structures are observed in CIDE family members involved in lipid homeostasis, and mutations on the charged interfaces compromise lipid droplet fusion, suggesting that CIDE domains represent a scaffold for higher-order assembly in DNA fragmentation and other biological processes such as lipid homeostasis.
CIDE domains form functionally important higher-order assemblies for DNA fragmentation.,Choi JY, Qiao Q, Hong SH, Kim CM, Jeong JH, Kim YG, Jung YK, Wu H, Park HH Proc Natl Acad Sci U S A. 2017 Jul 11;114(28):7361-7366. doi:, 10.1073/pnas.1705949114. Epub 2017 Jun 26. PMID:28652364[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Choi JY, Qiao Q, Hong SH, Kim CM, Jeong JH, Kim YG, Jung YK, Wu H, Park HH. CIDE domains form functionally important higher-order assemblies for DNA fragmentation. Proc Natl Acad Sci U S A. 2017 Jul 11;114(28):7361-7366. doi:, 10.1073/pnas.1705949114. Epub 2017 Jun 26. PMID:28652364 doi:http://dx.doi.org/10.1073/pnas.1705949114
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