3v6m: Difference between revisions

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-'''Unreleased structure'''
-The entry 3v6m is ON HOLD  until Paper Publication
+==Inhibition of caspase-6 activity by single mutation outside the active site==
+<StructureSection load='3v6m' size='340' side='right'caption='[[3v6m]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3v6m]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3V6M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3V6M 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]] 2.692&#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=3v6m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3v6m OCA], [https://pdbe.org/3v6m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3v6m RCSB], [https://www.ebi.ac.uk/pdbsum/3v6m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3v6m ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CASP6_HUMAN CASP6_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves poly(ADP-ribose) polymerase in vitro, as well as lamins. Overexpression promotes programmed cell death.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The apoptotic effector caspase-6 (CASP6) has been clearly identified as a drug target due to its strong association with neurodegeneration and axonal pruning events as well as its crucial roles in Huntington disease and Alzheimer disease. CASP6 activity is suppressed by ARK5-mediated phosphorylation at Ser(257) with an unclear mechanism. In this work, we solved crystal structures of DeltaproCASP6S257E and p20/p10S257E, which mimicked the phosphorylated CASP6 zymogen and activated CASP6, respectively. The structural investigation combined with extensive biochemical assay and molecular dynamics simulation studies revealed that phosphorylation on Ser(257) inhibited self-activation of CASP6 zymogen by "locking" the enzyme in the TEVD(193)-bound "inhibited state." The structural and biochemical results also showed that phosphorylation on Ser(257) inhibited the CASP6 activity by steric hindrance. These results disclosed the inhibition mechanism of CASP6 phosphorylation and laid the foundation for a new strategy of rational CASP6 drug design.
-Authors: Cao, Q., Wang, X.J., Liu, D.F., Li, L.F., Su, X.D.
+Inhibitory mechanism of caspase-6 phosphorylation revealed by crystal structures, molecular dynamics simulations, and biochemical assays.,Cao Q, Wang XJ, Liu CW, Liu DF, Li LF, Gao YQ, Su XD J Biol Chem. 2012 May 4;287(19):15371-9. Epub 2012 Mar 20. PMID:22433863<ref>PMID:22433863</ref>
-Description: Inhibition of caspase-6 activity by single mutation outside the active site
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3v6m" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Caspase 3D structures|Caspase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Cao Q]]
+[[Category: Li LF]]
+[[Category: Liu DF]]
+[[Category: Su XD]]
+[[Category: Wang XJ]]