View source for 7v6e


==DREP3==
<StructureSection load='7v6e' size='340' side='right'caption='[[7v6e]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7v6e]] is a 9 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=7V6E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7V6E FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3&#8491;</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=7v6e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7v6e OCA], [https://pdbe.org/7v6e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7v6e RCSB], [https://www.ebi.ac.uk/pdbsum/7v6e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7v6e ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q0E9B7_DROME Q0E9B7_DROME] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The cell-death-inducing DFF45-like effector (CIDE) domain is a protein-interaction module comprising approximately 80 amino acids and was initially identified in several apoptotic nucleases and their regulators. CIDE-domain-containing proteins were subsequently identified among proteins involved in lipid metabolism. Given the involvement of CIDE-domain-containing proteins in cell death and lipid homeostasis, their structure and function have been intensively studied. Here, the head-to-tail helical filament structure of the CIDE domain of DNA fragmentation factor-related protein 3 (DREP3) is presented. The helical filament structure was formed by opposing positively and negatively charged interfaces of the domain and was assembled depending on protein and salt concentrations. Although conserved filament structures are observed in CIDE family members, the structure elucidated in this study and its comparison with previous structures indicated that the size and the number of molecules used in one turn vary. These findings suggest that this charged-surface-based head-to-tail helical filament structure represents a unified mechanism of CIDE-domain assembly and provides insight into the function of various forms of the filament structure of the CIDE domain in higher-order assembly for apoptotic DNA fragmentation and control of lipid-droplet size.

Helical filament structure of the DREP3 CIDE domain reveals a unified mechanism of CIDE-domain assembly.,Lee SY, Kwon S, Ha HJ, Lee SH, Park HH Acta Crystallogr D Struct Biol. 2021 Dec 1;77(Pt 12):1543-1553. doi:, 10.1107/S2059798321010767. Epub 2021 Nov 11. PMID:34866610<ref>PMID:34866610</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7v6e" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Lee SY]]
[[Category: Park HH]]