3uij - Revision history

OCA at 13:59, 14 March 2024

2024-03-14T13:59:42Z

←Older revision		Revision as of 13:59, 14 March 2024
Line 3:		Line 3:
	<StructureSection load='3uij' size='340' side='right'caption='[[3uij]], [[Resolution\|resolution]] 2.71Å' scene=''>		<StructureSection load='3uij' size='340' side='right'caption='[[3uij]], [[Resolution\|resolution]] 2.71Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3uij]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UIJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3uij]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UIJ 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]] 2.705Å</td></tr>
-	<tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'~~>~~[[3uig\|3uig]], [[3uih\|3uih]], [[3uii\|3uii]], [[3uik\|3uik]]~~<~~/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~~='~~gene'><td class~~=~~"sblockLbl"><b>[[Gene\|Gene~~:~~]]</b~~></td>~~<td class="sblockDat">BIRC5, API4, IAP4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])~~</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=3uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uij OCA], [https://pdbe.org/3uij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uij RCSB], [https://www.ebi.ac.uk/pdbsum/3uij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uij 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=3uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uij OCA], [https://pdbe.org/3uij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uij RCSB], [https://www.ebi.ac.uk/pdbsum/3uij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uij ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[https://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:[https://omim.org/entry/614152 614152]]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:21722859</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref> [[https://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.<ref>PMID:10929711</ref> <ref>PMID:14523016</ref> <ref>PMID:15200957</ref>	+	[https://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref>
-	~~<div style="background-color:#fffaf0;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Survivin is an inhibitor of apoptosis family protein implicated in apoptosis and mitosis. In apoptosis, it has been shown to recognize the Smac/DIABLO protein. It is also a component of the chromosomal passenger complex, a key player during mitosis. Recently, Survivin was identified in vitro and in vivo as the direct binding partner for phosphorylated Thr3 on histone H3 (H3T3ph). We have undertaken structural and binding studies to investigate the molecular basis underlying recognition of H3T3ph and Smac/DIABLO N-terminal peptides by Survivin. Our crystallographic studies establish recognition of N-terminal Ala in both complexes and identify intermolecular hydrogen-bonding interactions in the Survivin phosphate-binding pocket that contribute to H3T3ph mark recognition. In addition, our calorimetric data establish that Survivin binds tighter to the H3T3ph-containing peptide relative to the N-terminal Smac/DIABLO peptide, and this preference can be reversed through structure-guided mutations that increase the hydrophobicity of the phosphate-binding pocket.	+
-		+
-	Structural Basis for Recognition of H3T3ph and Smac/DIABLO N-terminal Peptides by Human Survivin.,Du J, Kelly AE, Funabiki H, Patel DJ Structure. 2012 Jan 11;20(1):185-95. PMID:22244766<ref>PMID:22244766</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3uij" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 29:		Line 17:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Du, J]]	+	[[Category: Du J]]
-	[[Category: Patel~~, D J]]~~	+	[[Category: Patel DJ]]
-	~~[[Category: Apoptosis-apoptosis inhibitor complex]]~~	+
-	~~[[Category: Bir domain]]~~	+
-	~~[[Category: Mitosis]]~~	+
-	~~[[Category: Smac/diablo binding]]~~	+
-	~~[[Category: T3 phosphorylated h3 binding~~]]	+

OCA at 07:37, 20 July 2022

2022-07-20T07:37:50Z

←Older revision		Revision as of 07:37, 20 July 2022
Line 1:		Line 1:

	==Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide==		==Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide==
-	<StructureSection load='3uij' size='340' side='right' caption='[[3uij]], [[Resolution\|resolution]] 2.71Å' scene=''>	+	<StructureSection load='3uij' size='340' side='right'caption='[[3uij]], [[Resolution\|resolution]] 2.71Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3uij]] is a 4 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=3UIJ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3UIJ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3uij]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UIJ FirstGlance]. <br>
-	</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>	+	</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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3uig\|3uig]], [[3uih\|3uih]], [[3uii\|3uii]], [[3uik\|3uik]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3uig\|3uig]], [[3uih\|3uih]], [[3uii\|3uii]], [[3uik\|3uik]]</div></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BIRC5, API4, IAP4 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BIRC5, API4, IAP4 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uij OCA], [~~http~~://pdbe.org/3uij PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3uij RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3uij PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3uij 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=3uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uij OCA], [https://pdbe.org/3uij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uij RCSB], [https://www.ebi.ac.uk/pdbsum/3uij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uij ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:[~~http~~://omim.org/entry/614152 614152]]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:21722859</ref>	+	[[https://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:[https://omim.org/entry/614152 614152]]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:21722859</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref> [[~~http~~://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.<ref>PMID:10929711</ref> <ref>PMID:14523016</ref> <ref>PMID:15200957</ref>	+	[[https://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref> [[https://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.<ref>PMID:10929711</ref> <ref>PMID:14523016</ref> <ref>PMID:15200957</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 30:		Line 30:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Du, J]]		[[Category: Du, J]]
	[[Category: Patel, D J]]		[[Category: Patel, D J]]

OCA at 21:38, 5 August 2016

2016-08-05T21:38:03Z

←Older revision		Revision as of 21:38, 5 August 2016
Line 1:		Line 1:
-	{{STRUCTURE_3uij\| PDB=3uij \| SCENE= }}
-	===Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide===
-	{{ABSTRACT_PUBMED_22244766}}

-	==Disease==	+	==Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide==
-	[[http://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:[http://omim.org/entry/614152 614152]]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:21722859</ref>	+	<StructureSection load='3uij' size='340' side='right' caption='[[3uij]], [[Resolution\|resolution]] 2.71Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3uij]] is a 4 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=3UIJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3UIJ FirstGlance]. <br>
		+	</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>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3uig\|3uig]], [[3uih\|3uih]], [[3uii\|3uii]], [[3uik\|3uik]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">BIRC5, API4, IAP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3uij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uij OCA], [http://pdbe.org/3uij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3uij RCSB], [http://www.ebi.ac.uk/pdbsum/3uij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3uij ProSAT]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:[http://omim.org/entry/614152 614152]]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:21722859</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref> <ref>PMID:9859993</ref> <ref>PMID:12773388</ref> <ref>PMID:16322459</ref> <ref>PMID:16291752</ref> <ref>PMID:18591255</ref> <ref>PMID:20826784</ref> <ref>PMID:21536684</ref> [[http://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.<ref>PMID:10929711</ref> <ref>PMID:14523016</ref> <ref>PMID:15200957</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Survivin is an inhibitor of apoptosis family protein implicated in apoptosis and mitosis. In apoptosis, it has been shown to recognize the Smac/DIABLO protein. It is also a component of the chromosomal passenger complex, a key player during mitosis. Recently, Survivin was identified in vitro and in vivo as the direct binding partner for phosphorylated Thr3 on histone H3 (H3T3ph). We have undertaken structural and binding studies to investigate the molecular basis underlying recognition of H3T3ph and Smac/DIABLO N-terminal peptides by Survivin. Our crystallographic studies establish recognition of N-terminal Ala in both complexes and identify intermolecular hydrogen-bonding interactions in the Survivin phosphate-binding pocket that contribute to H3T3ph mark recognition. In addition, our calorimetric data establish that Survivin binds tighter to the H3T3ph-containing peptide relative to the N-terminal Smac/DIABLO peptide, and this preference can be reversed through structure-guided mutations that increase the hydrophobicity of the phosphate-binding pocket.

-	~~==Function==~~	+	Structural Basis for Recognition of H3T3ph and Smac/DIABLO N-terminal Peptides by Human Survivin.,Du J, Kelly AE, Funabiki H, Patel DJ Structure. 2012 Jan 11;20(1):185-95. PMID:22244766<ref>PMID:22244766</ref>
-	[[http://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for ~~chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator~~ of ~~the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis~~ and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-~~apoptotic effects when compared with the displayed wild-type isoform~~.<ref>PMID:10626797</ref><ref>PMID:9859993</ref><ref>PMID:12773388</ref><ref>PMID:16322459</ref><ref>PMID:16291752</ref><ref>PMID:18591255</ref><ref>PMID:20826784</ref><ref>PMID:21536684</ref> [[http://www.~~uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-~~1~~/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP~~). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-~~proteasome pathway~~. ~~Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.<ref>~~PMID:~~10929711</ref><ref>PMID:14523016</ref>~~<ref>PMID:~~15200957~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[3uij]] is~~ a ~~4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca~~-~~bin~~/~~ocashort?id=3UIJ OCA].~~	+	</div>
		+	<div class="pdbe-citations 3uij" style="background-color:#fffaf0;"></div>

-	==~~Reference~~==	+	==See Also==
-	~~<ref group~~=~~"xtra">PMID:022244766</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	*[[Survivin\|Survivin]]
-	[[Category: ~~Homo sapiens~~]]	+	== References ==
-	[[Category: Du, J.]]	+	<references/>
-	[[Category: Patel, D J.]]	+	__TOC__
		+	</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Du, J]]
		+	[[Category: Patel, D J]]
	[[Category: Apoptosis-apoptosis inhibitor complex]]		[[Category: Apoptosis-apoptosis inhibitor complex]]
	[[Category: Bir domain]]		[[Category: Bir domain]]

OCA at 05:53, 25 March 2013

2013-03-25T05:53:31Z

←Older revision		Revision as of 05:53, 25 March 2013
Line 1:		Line 1:
-	[[Image:3uij.png\|left\|200px]]
-
	{{STRUCTURE_3uij\| PDB=3uij \| SCENE= }}		{{STRUCTURE_3uij\| PDB=3uij \| SCENE= }}
-
	===Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide===		===Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide===
		+	{{ABSTRACT_PUBMED_22244766}}

-	~~{{ABSTRACT_PUBMED_22244766}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Defects in DIABLO are the cause of deafness autosomal dominant type 64 (DFNA64) [MIM:[http://omim.org/entry/614152 614152]]. DFNA64 is a form of non-syndromic sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.<ref>PMID:21722859</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/BIRC5_HUMAN BIRC5_HUMAN]] Multitasking protein that has dual roles in promoting cell proliferation and preventing apoptosis. Component of a chromosome passage protein complex (CPC) which is essential for chromosome alignment and segregation during mitosis and cytokinesis. Acts as an important regulator of the localization of this complex; directs CPC movement to different locations from the inner centromere during prometaphase to midbody during cytokinesis and participates in the organization of the center spindle by associating with polymerized microtubules. The complex with RAN plays a role in mitotic spindle formation by serving as a physical scaffold to help deliver the RAN effector molecule TPX2 to microtubules. May counteract a default induction of apoptosis in G2/M phase. The acetylated form represses STAT3 transactivation of target gene promoters. May play a role in neoplasia. Inhibitor of CASP3 and CASP7. Isoform 2 and isoform 3 do not appear to play vital roles in mitosis. Isoform 3 shows a marked reduction in its anti-apoptotic effects when compared with the displayed wild-type isoform.<ref>PMID:10626797</ref><ref>PMID:9859993</ref><ref>PMID:12773388</ref><ref>PMID:16322459</ref><ref>PMID:16291752</ref><ref>PMID:18591255</ref><ref>PMID:20826784</ref><ref>PMID:21536684</ref> [[http://www.uniprot.org/uniprot/DBLOH_HUMAN DBLOH_HUMAN]] Promotes apoptosis by activating caspases in the cytochrome c/Apaf-1/caspase-9 pathway. Acts by opposing the inhibitory activity of inhibitor of apoptosis proteins (IAP). Inhibits the activity of BIRC6/bruce by inhibiting its binding to caspases. Isoform 3 attenuates the stability and apoptosis-inhibiting activity of XIAP/BIRC4 by promoting XIAP/BIRC4 ubiquitination and degradation through the ubiquitin-proteasome pathway. Isoform 3 also disrupts XIAP/BIRC4 interacting with processed caspase-9 and promotes caspase-3 activation. Isoform 1 is defective in the capacity to down-regulate the XIAP/BIRC4 abundance.<ref>PMID:10929711</ref><ref>PMID:14523016</ref><ref>PMID:15200957</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:022244766</ref><references group="xtra"/>	+	<ref group="xtra">PMID:022244766</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Du, J.]]		[[Category: Du, J.]]

OCA at 10:13, 8 August 2012

2012-08-08T10:13:24Z

←Older revision		Revision as of 10:13, 8 August 2012
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-	[[Image:3uij.~~jpg~~\|left\|200px]]	+	[[Image:3uij.png\|left\|200px]]

-	<!--
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	{{STRUCTURE_3uij\| PDB=3uij \| SCENE= }}		{{STRUCTURE_3uij\| PDB=3uij \| SCENE= }}

	===Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide===		===Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_22244766}}, adds the Publication Abstract to the page
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	{{ABSTRACT_PUBMED_22244766}}		{{ABSTRACT_PUBMED_22244766}}

OCA at 07:16, 1 February 2012

2012-02-01T07:16:08Z

←Older revision		Revision as of 07:16, 1 February 2012
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-	~~'''Unreleased structure'''~~	+	[[Image:3uij.jpg\|left\|200px]]

-	The ~~entry 3uij~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	<!--
		+	The line below this paragraph, containing "STRUCTURE_3uij", creates the "Structure Box" on the page.
		+	You may change the PDB parameter (which sets the PDB file loaded into the applet)
		+	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
		+	or leave the SCENE parameter empty for the default display.
		+	-->
		+	{{STRUCTURE_3uij\| PDB=3uij \| SCENE= }}

-	~~Authors: Du, J., Patel, D.J.~~	+	===Crystal structure of human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide===

-	~~Description~~: ~~crystal~~ structure ~~human Survivin K62Y~~/~~H80W mutant in~~ complex ~~with~~ Smac/~~DIABLO(1-15) peptide~~	+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_22244766}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 22244766 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_22244766}}
		+
		+	==About this Structure==
		+	[[3uij]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3UIJ OCA].
		+
		+	==Reference==
		+	<ref group="xtra">PMID:022244766</ref><references group="xtra"/>
		+	[[Category: Homo sapiens]]
		+	[[Category: Du, J.]]
		+	[[Category: Patel, D J.]]
		+	[[Category: Apoptosis-apoptosis inhibitor complex]]
		+	[[Category: Bir domain]]
		+	[[Category: Mitosis]]
		+	[[Category: Smac/diablo binding]]
		+	[[Category: T3 phosphorylated h3 binding]]

OCA: Protected "3uij" [edit=sysop:move=sysop]

2011-11-16T11:54:14Z

Protected "3uij" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:54, 16 November 2011

OCA: New page: '''Unreleased structure''' The entry 3uij is ON HOLD until Paper Publication Authors: Du, J., Patel, D.J. Description: crystal structure human Survivin K62Y/H80W mutant in complex with...

2011-11-16T11:54:13Z

New page: '''Unreleased structure''' The entry 3uij is ON HOLD until Paper Publication Authors: Du, J., Patel, D.J. Description: crystal structure human Survivin K62Y/H80W mutant in complex with...

New page

'''Unreleased structure'''

The entry 3uij is ON HOLD until Paper Publication

Authors: Du, J., Patel, D.J.

Description: crystal structure human Survivin K62Y/H80W mutant in complex with Smac/DIABLO(1-15) peptide