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| | <StructureSection load='3sip' size='340' side='right'caption='[[3sip]], [[Resolution|resolution]] 3.50Å' scene=''> | | <StructureSection load='3sip' size='340' side='right'caption='[[3sip]], [[Resolution|resolution]] 3.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3sip]] is a 6 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=3SIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SIP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3sip]] is a 6 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=3SIP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SIP FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.496Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3siq|3siq]]</div></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> |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3sip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sip OCA], [https://pdbe.org/3sip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sip RCSB], [https://www.ebi.ac.uk/pdbsum/3sip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sip ProSAT]</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=3sip FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sip OCA], [https://pdbe.org/3sip PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sip RCSB], [https://www.ebi.ac.uk/pdbsum/3sip PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sip ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/ICE_DROME ICE_DROME]] Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro. [[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/DRICE_DROME DRICE_DROME] Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Li, X]] | + | [[Category: Li X]] |
| - | [[Category: Shi, Y]] | + | [[Category: Shi Y]] |
| - | [[Category: Wang, J]] | + | [[Category: Wang J]] |
| - | [[Category: Bir domain]]
| + | |
| - | [[Category: Caspase]]
| + | |
| - | [[Category: Hydrolase-ligase-hydrolase complex]]
| + | |
| Structural highlights
Function
DRICE_DROME Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro.
Publication Abstract from PubMed
The Drosophila inhibitor of apoptosis protein DIAP1 exists in an auto-inhibited conformation, unable to suppress the effector caspase drICE. Auto-inhibition is disabled by caspase-mediated cleavage of DIAP1 after Asp20. The cleaved DIAP1 binds to mature drICE, inhibits its protease activity, and, presumably, also targets drICE for ubiquitylation. DIAP1-mediated suppression of drICE is effectively antagonized by the pro-apoptotic proteins Reaper, Hid, and Grim (RHG). Despite rigorous effort, the molecular mechanisms behind these observations are enigmatic. Here we report a 2.4 A crystal structure of uncleaved DIAP1-BIR1, which reveals how the amino-terminal sequences recognize a conserved surface groove in BIR1 to achieve auto-inhibition, and a 3.5 A crystal structure of active drICE bound to cleaved DIAP1-BIR1, which provides a structural explanation to DIAP1-mediated inhibition of drICE. These structures and associated biochemical analyses, together with published reports, define the molecular determinants that govern the interplay among DIAP1, drICE and the RHG proteins.
Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE.,Li X, Wang J, Shi Y Nat Commun. 2011 Aug 2;2:408. doi: 10.1038/ncomms1418. PMID:21811237[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Li X, Wang J, Shi Y. Structural mechanisms of DIAP1 auto-inhibition and DIAP1-mediated inhibition of drICE. Nat Commun. 2011 Aug 2;2:408. doi: 10.1038/ncomms1418. PMID:21811237 doi:10.1038/ncomms1418
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