1jd4: Difference between revisions
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==Crystal Structure of DIAP1-BIR2== | ==Crystal Structure of DIAP1-BIR2== | ||
<StructureSection load='1jd4' size='340' side='right' caption='[[1jd4]], [[Resolution|resolution]] 2.70Å' scene=''> | <StructureSection load='1jd4' size='340' side='right' caption='[[1jd4]], [[Resolution|resolution]] 2.70Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jd5|1jd5]], [[1jd6|1jd6]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1jd5|1jd5]], [[1jd6|1jd6]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DIAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DIAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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=1jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jd4 OCA], [http://pdbe.org/1jd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jd4 RCSB], [http://www.ebi.ac.uk/pdbsum/1jd4 PDBsum]</span></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=1jd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jd4 OCA], [http://pdbe.org/1jd4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jd4 RCSB], [http://www.ebi.ac.uk/pdbsum/1jd4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jd4 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jd4 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 12:58, 4 October 2017
Crystal Structure of DIAP1-BIR2Crystal Structure of DIAP1-BIR2
Structural highlights
Function[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.[1] [2] [3] [4] [5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe inhibitor of apoptosis protein DIAP1 suppresses apoptosis in Drosophila, with the second BIR domain (BIR2) playing an important role. Three proteins, Hid, Grim, and Reaper, promote apoptosis, in part by binding to DIAP1 through their conserved N-terminal sequences. The crystal structures of DIAP1-BIR2 by itself and in complex with the N-terminal peptides from Hid and Grim reveal that these peptides bind a surface groove on DIAP1, with the first four amino acids mimicking the binding of the Smac tetrapeptide to XIAP. The next 3 residues also contribute to binding through hydrophobic interactions. Interestingly, peptide binding induces the formation of an additional alpha helix in DIAP1. Our study reveals the structural conservation and diversity necessary for the binding of IAPs by the Drosophila Hid/Grim/Reaper and the mammalian Smac proteins. Structural analysis of a functional DIAP1 fragment bound to grim and hid peptides.,Wu JW, Cocina AE, Chai J, Hay BA, Shi Y Mol Cell. 2001 Jul;8(1):95-104. PMID:11511363[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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