View source for 3sir


==Crystal Structure of drICE==
<StructureSection load='3sir' size='340' side='right'caption='[[3sir]], [[Resolution|resolution]] 2.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3sir]] is a 4 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=3SIR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SIR 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]] 2.68&#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=3sir FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sir OCA], [https://pdbe.org/3sir PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sir RCSB], [https://www.ebi.ac.uk/pdbsum/3sir PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sir ProSAT]</span></td></tr>
</table>
== Function ==
[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.
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== 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<ref>PMID:21811237</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3sir" style="background-color:#fffaf0;"></div>

==See Also==
*[[Caspase 3D structures|Caspase 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Drosophila melanogaster]]
[[Category: Large Structures]]
[[Category: Li X]]
[[Category: Shi Y]]
[[Category: Wang J]]