1q4q

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<StructureSection load='1q4q' size='340' side='right'caption='[[1q4q]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='1q4q' size='340' side='right'caption='[[1q4q]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1q4q]] is a 20 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4Q OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q4Q FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1q4q]] is a 20 chain structure with sequence from [https://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q4Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q4Q FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jd4|1jd4]], [[1jd5|1jd5]], [[1jd6|1jd6]]</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jd4|1jd4]], [[1jd5|1jd5]], [[1jd6|1jd6]]</div></td></tr>
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<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=1q4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q4q OCA], [http://pdbe.org/1q4q PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1q4q RCSB], [http://www.ebi.ac.uk/pdbsum/1q4q PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1q4q ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1q4q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q4q OCA], [https://pdbe.org/1q4q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q4q RCSB], [https://www.ebi.ac.uk/pdbsum/1q4q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q4q ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/IAP1_DROME IAP1_DROME]] Anti-apoptotic protein which functions as a caspase regulator, using its E3 ubiquitin-protein ligase activity to smother caspase activity. Binds, ubiquitinates and inactivates initiator caspase Nc, and effector caspases ICE and DCP-1. Acts as a NEDD8-E3 ubiquitin-protein ligase for ICE. Suppresses apoptosis by targeting the apoptosome for ubiquitination and inactivation. Plays an important role in cell motility. Overexpression suppresses rpr and W-dependent cell death in the eye. Interaction of th with Nc is required to suppress Nc-mediated cell death; th-mediated ubiquitination of Nc. Acts as a positive regulator of Wnt signaling.<ref>PMID:8548811</ref> <ref>PMID:17397804</ref> <ref>PMID:18259196</ref> <ref>PMID:21145488</ref> <ref>PMID:22304967</ref> <ref>PMID:14517550</ref> [[http://www.uniprot.org/uniprot/ICENC_DROME ICENC_DROME]] Involved in the activation cascade of caspases responsible for apoptosis execution. Effector of steroid-mediated apoptosis during insect metamorphosis. Overexpression promotes programmed cell death. Interaction with th is required to suppress Nc-mediated cell death; via th-mediated ubiquitination of Nc. Rate-limiting caspase in rpr and W death pathway.<ref>PMID:10200258</ref> <ref>PMID:10675329</ref> <ref>PMID:10984473</ref> <ref>PMID:14517550</ref>
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[[https://www.uniprot.org/uniprot/IAP1_DROME IAP1_DROME]] Anti-apoptotic protein which functions as a caspase regulator, using its E3 ubiquitin-protein ligase activity to smother caspase activity. Binds, ubiquitinates and inactivates initiator caspase Nc, and effector caspases ICE and DCP-1. Acts as a NEDD8-E3 ubiquitin-protein ligase for ICE. Suppresses apoptosis by targeting the apoptosome for ubiquitination and inactivation. Plays an important role in cell motility. Overexpression suppresses rpr and W-dependent cell death in the eye. Interaction of th with Nc is required to suppress Nc-mediated cell death; th-mediated ubiquitination of Nc. Acts as a positive regulator of Wnt signaling.<ref>PMID:8548811</ref> <ref>PMID:17397804</ref> <ref>PMID:18259196</ref> <ref>PMID:21145488</ref> <ref>PMID:22304967</ref> <ref>PMID:14517550</ref> [[https://www.uniprot.org/uniprot/ICENC_DROME ICENC_DROME]] Involved in the activation cascade of caspases responsible for apoptosis execution. Effector of steroid-mediated apoptosis during insect metamorphosis. Overexpression promotes programmed cell death. Interaction with th is required to suppress Nc-mediated cell death; via th-mediated ubiquitination of Nc. Rate-limiting caspase in rpr and W death pathway.<ref>PMID:10200258</ref> <ref>PMID:10675329</ref> <ref>PMID:10984473</ref> <ref>PMID:14517550</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 16:14, 27 October 2021

Crystal structure of a DIAP1-Dronc complex

PDB ID 1q4q

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