4d2k: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4d2k]] is a 4 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=4D2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2K FirstGlance]. <br> | <table><tr><td colspan='2'>[[4d2k]] is a 4 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=4D2K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4D2K FirstGlance]. <br> | ||
</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=4d2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2k OCA], [https://pdbe.org/4d2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2k RCSB], [https://www.ebi.ac.uk/pdbsum/4d2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2k ProSAT]</span></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]] 2.302Å</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=4d2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4d2k OCA], [https://pdbe.org/4d2k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4d2k RCSB], [https://www.ebi.ac.uk/pdbsum/4d2k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4d2k ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/Q7K304_DROME Q7K304_DROME] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Latest revision as of 15:19, 20 December 2023
Crystal structure of DREP2 CIDE domainCrystal structure of DREP2 CIDE domain
Structural highlights
FunctionPublication Abstract from PubMedCell 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
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