2cnn: Difference between revisions

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==Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors.==
==Crystal structures of caspase-3 in complex with aza-peptide epoxide inhibitors.==
<StructureSection load='2cnn' size='340' side='right' caption='[[2cnn]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='2cnn' size='340' side='right'caption='[[2cnn]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2cnn]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2CNN FirstGlance]. <br>
<table><tr><td colspan='2'>[[2cnn]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CNN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CNN FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MY5:{1-[(3S)-4-{[(1S)-2-(BENZYLAMINO)-1-METHYL-2-OXOETHYL]AMINO}-3-HYDROXY-4-OXOBUTANOYL]HYDRAZINO}ACETIC+ACID'>MY5</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</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]] 1.7&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cp3|1cp3]], [[1gfw|1gfw]], [[1i3o|1i3o]], [[1nme|1nme]], [[1nmq|1nmq]], [[1nms|1nms]], [[1pau|1pau]], [[1qx3|1qx3]], [[1re1|1re1]], [[1rhj|1rhj]], [[1rhk|1rhk]], [[1rhm|1rhm]], [[1rhq|1rhq]], [[1rhr|1rhr]], [[1rhu|1rhu]], [[2c1e|2c1e]], [[2c2k|2c2k]], [[2c2m|2c2m]], [[2c2o|2c2o]], [[2cdr|2cdr]], [[2cjx|2cjx]], [[2cjy|2cjy]], [[2cnk|2cnk]], [[2cnl|2cnl]], [[2cno|2cno]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABN:BENZYLAMINE'>ABN</scene>, <scene name='pdbligand=MY0:(2S)-4-[1-(CARBOXYMETHYL)HYDRAZINYL]-2-HYDROXY-4-OXOBUTANOIC+ACID'>MY0</scene>, <scene name='pdbligand=PHQ:BENZYL+CHLOROCARBONATE'>PHQ</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=2cnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnn OCA], [http://pdbe.org/2cnn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cnn RCSB], [http://www.ebi.ac.uk/pdbsum/2cnn PDBsum]</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=2cnn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cnn OCA], [https://pdbe.org/2cnn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2cnn RCSB], [https://www.ebi.ac.uk/pdbsum/2cnn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2cnn ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CASP3_HUMAN CASP3_HUMAN]] Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.<ref>PMID:7596430</ref> <ref>PMID:21357690</ref>
[https://www.uniprot.org/uniprot/CASP3_HUMAN CASP3_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage.<ref>PMID:7596430</ref> <ref>PMID:21357690</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/2cnn_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cn/2cnn_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </jmolCheckbox>
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==See Also==
==See Also==
*[[Caspase|Caspase]]
*[[Caspase 3D structures|Caspase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Asgian, J L]]
[[Category: Large Structures]]
[[Category: Campbell, A J]]
[[Category: Synthetic construct]]
[[Category: Ganesan, R]]
[[Category: Asgian JL]]
[[Category: Grutter, M G]]
[[Category: Campbell AJ]]
[[Category: Jelakovic, S]]
[[Category: Ganesan R]]
[[Category: Li, Z Z]]
[[Category: Grutter MG]]
[[Category: Powers, J C]]
[[Category: Jelakovic S]]
[[Category: Apoptosis]]
[[Category: Li ZZ]]
[[Category: Aza-asp]]
[[Category: Powers JC]]
[[Category: Aza-peptide]]
[[Category: Clan cd]]
[[Category: Cpp32]]
[[Category: Cysteine-protease]]
[[Category: Epoxide]]
[[Category: Epoxysuccinyl]]
[[Category: Hydrolase-hydrolase inhibitor complex]]
[[Category: Ice]]
[[Category: Phosphorylation]]
[[Category: Protease]]
[[Category: Protease-inhibitor complex]]
[[Category: Tetramer]]
[[Category: Thiol protease]]
[[Category: Yama]]
[[Category: Zymogen]]

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