3nr2: Difference between revisions

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-'''Unreleased structure'''
-The entry 3nr2 is ON HOLD  until Paper Publication
+==Crystal structure of Caspase-6 zymogen==
+<StructureSection load='3nr2' size='340' side='right'caption='[[3nr2]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[3nr2]] is a 2 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=3NR2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3NR2 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]] 2.9&#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=3nr2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nr2 OCA], [https://pdbe.org/3nr2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3nr2 RCSB], [https://www.ebi.ac.uk/pdbsum/3nr2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3nr2 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 ==
+Dimeric effectors caspase 3 and caspase 7 are activated by initiator caspase processing. In this study, we report the crystal structures of effector caspase 6 (CASP6) zymogen and N-Acetyl-Val-Glu-Ile-Asp-al-inhibited CASP6. Both of these forms of CASP6 have a dimeric structure, and in CASP6 zymogen the intersubunit cleavage site (190)TEVD(193) is well structured and inserts into the active site. This positions residue Asp 193 to be easily attacked by the catalytic residue Cys 163. We demonstrate biochemically that intramolecular cleavage at Asp 193 is a prerequisite for CASP6 self-activation and that this activation mechanism is dependent on the length of the L2 loop. Our results indicate that CASP6 can be activated and regulated through intramolecular self-cleavage.
-Authors: Su, X.-D., Wang, X.J., Liu, X., Mi, W., Wang, K.T.
+Crystal structures of human caspase 6 reveal a new mechanism for intramolecular cleavage self-activation.,Wang XJ, Cao Q, Liu X, Wang KT, Mi W, Zhang Y, Li LF, Leblanc AC, Su XD EMBO Rep. 2010 Oct 1. PMID:20890311<ref>PMID:20890311</ref>
-Description: Crystal structure of Caspase-6 zymogen
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 3nr2" style="background-color:#fffaf0;"></div>
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 14 16:08:31 2010''
+==See Also==
+*[[Caspase 3D structures|Caspase 3D structures]]
+*[[Caspase-6 and neurodegeneration|Caspase-6 and neurodegeneration]]
+*[[Molecular Playground/Caspase-6 and neurodegeneration|Molecular Playground/Caspase-6 and neurodegeneration]]
+*[[User:Kevin Buadlart Dagbay|User:Kevin Buadlart Dagbay]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Liu X]]
+[[Category: Mi W]]
+[[Category: Su X-D]]
+[[Category: Wang K-T]]
+[[Category: Wang X-J]]