3zjg - Revision history

OCA at 11:03, 20 December 2023

OCA — Wed, 20 Dec 2023 11:03:11 GMT

←Older revision		Revision as of 11:03, 20 December 2023
Line 3:		Line 3:
	<StructureSection load='3zjg' size='340' side='right'caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3zjg' size='340' side='right'caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zjg]] is a 2 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=3ZJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZJG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zjg]] is a 2 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=3ZJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZJG FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=CL:CHLORIDE+ION'>CL</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]] 1.92Å</td></tr>
-	<tr id='~~NonStdRes~~'><td class="sblockLbl"><b>[[~~Non-Standard_Residue~~\|~~NonStd Res~~:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene~~></td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zjd\|3zjd]], [[3zje\|3zje]], [[3zjf\|3zjf]]</div~~></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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [https://pdbe.org/3zjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [https://www.ebi.ac.uk/pdbsum/3zjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zjg 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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [https://pdbe.org/3zjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [https://www.ebi.ac.uk/pdbsum/3zjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zjg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN]] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>	+	[https://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>
	<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: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Arnaudo, N]]	+	[[Category: Arnaudo N]]
-	[[Category: Barford, D]]	+	[[Category: Barford D]]
-	[[Category: Busch, M]]	+	[[Category: Busch M]]
-	[[Category: Carroll~~, K S~~]]	+	[[Category: Carroll KS]]
-	[[Category: Garcia~~, F J~~]]	+	[[Category: Garcia FJ]]
-	[[Category: Komander, D]]	+	[[Category: Komander D]]
-	[[Category: Kulathu, Y]]	+	[[Category: Kulathu Y]]
-	[[Category: Mevissen~~, T E.T]]~~	+	[[Category: Mevissen TET]]
-	~~[[Category: Cys protease]]~~	+
-	~~[[Category: Deubiquitinating enzyme]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Reversible oxidation]]~~	+
-	~~[[Category: Sulphenic acid]]~~	+
-	~~[[Category: Sulphinic acid]]~~	+
-	~~[[Category: Sulphonic acid]]~~	+
-	~~[[Category: Ubiquitin~~]]	+

OCA at 05:48, 10 August 2022

OCA — Wed, 10 Aug 2022 05:48:29 GMT

←Older revision		Revision as of 05:48, 10 August 2022
Line 1:		Line 1:

	==A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.==		==A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.==
-	<StructureSection load='3zjg' size='340' side='right' caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>	+	<StructureSection load='3zjg' size='340' side='right'caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zjg]] is a 2 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=3ZJG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3ZJG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zjg]] is a 2 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=3ZJG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZJG FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zjd\|3zjd]], [[3zje\|3zje]], [[3zjf\|3zjf]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3zjd\|3zjd]], [[3zje\|3zje]], [[3zjf\|3zjf]]</div></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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [~~http~~://pdbe.org/3zjg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3zjg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3zjg 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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [https://pdbe.org/3zjg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [https://www.ebi.ac.uk/pdbsum/3zjg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zjg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN]] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>	+	[[https://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN]] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Arnaudo, N]]		[[Category: Arnaudo, N]]
	[[Category: Barford, D]]		[[Category: Barford, D]]

OCA at 17:20, 5 August 2016

OCA — Fri, 05 Aug 2016 17:20:20 GMT

←Older revision		Revision as of 17:20, 5 August 2016
Line 1:		Line 1:
		+
	==A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.==		==A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.==
	<StructureSection load='3zjg' size='340' side='right' caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3zjg' size='340' side='right' caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>
Line 6:		Line 7:
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zjd\|3zjd]], [[3zje\|3zje]], [[3zjf\|3zjf]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zjd\|3zjd]], [[3zje\|3zje]], [[3zjf\|3zjf]]</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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [http://www.ebi.ac.uk/pdbsum/3zjg 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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [http://pdbe.org/3zjg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [http://www.ebi.ac.uk/pdbsum/3zjg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3zjg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 3zjg" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:35, 25 December 2014

OCA — Thu, 25 Dec 2014 20:35:50 GMT

←Older revision		Revision as of 20:35, 25 December 2014
Line 2:		Line 2:
	<StructureSection load='3zjg' size='340' side='right' caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>		<StructureSection load='3zjg' size='340' side='right' caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3zjg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZJG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3zjg]] is a 2 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=3ZJG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZJG FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
Line 8:		Line 8:
	<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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [http://www.ebi.ac.uk/pdbsum/3zjg 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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [http://www.ebi.ac.uk/pdbsum/3zjg PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TNAP3_HUMAN TNAP3_HUMAN]] Ubiquitin-editing enzyme that contains both ubiquitin ligase and deubiquitinase activities. Involved in immune and inflammatory responses signaled by cytokines, such as TNF-alpha and IL-1 beta, or pathogens via Toll-like receptors (TLRs) through terminating NF-kappa-B activity. Essential component of a ubiquitin-editing protein complex, comprising also RNF11, ITCH and TAX1BP1, that ensures the transient nature of inflammatory signaling pathways. In cooperation with TAX1BP1 promotes disassembly of E2-E3 ubiquitin protein ligase complexes in IL-1R and TNFR-1 pathways; affected are at least E3 ligases TRAF6, TRAF2 and BIRC2, and E2 ubiquitin-conjugating enzymes UBE2N and UBE2D3. In cooperation with TAX1BP1 promotes ubiquitination of UBE2N and proteasomal degradation of UBE2N and UBE2D3. Upon TNF stimulation, deubiquitinates 'Lys-63'-polyubiquitin chains on RIPK1 and catalyzes the formation of 'Lys-48'-polyubiquitin chains. This leads to RIPK1 proteasomal degradation and consequently termination of the TNF- or LPS-mediated activation of NF-kappa-B. Deubiquinates TRAF6 probably acting on 'Lys-63'-linked polyubiquitin. Upon T-cell receptor (TCR)-mediated T-cell activation, deubiquitinates 'Lys-63'-polyubiquitin chains on MALT1 thereby mediating disassociation of the CBM (CARD11:BCL10:MALT1) and IKK complexes and preventing sustained IKK activation. Deubiquinates NEMO/IKBKG; the function is facilitated by TNIP1 and leads to inhibition of NF-kappa-B activation. Upon stimulation by bacterial peptidoglycans, probably deubiquitinates RIPK2. Can also inhibit I-kappa-B-kinase (IKK) through a non-catalytic mechanism which involves polyubiquitin; polyubiquitin promotes association with IKBKG and prevents IKK MAP3K7-mediated phosphorylation. Targets TRAF2 for lysosomal degradation. In vitro able to deubiquitinate both 'Lys-48'- and 'Lys-63' polyubiquitin chains. Inhibitor of programmed cell death. Has a role in the function of the lymphoid system.<ref>PMID:8692885</ref> <ref>PMID:9299557</ref> <ref>PMID:9882303</ref> <ref>PMID:14748687</ref> <ref>PMID:15258597</ref> <ref>PMID:16684768</ref> <ref>PMID:18952128</ref> <ref>PMID:19494296</ref> <ref>PMID:22099304</ref> <ref>PMID:17961127</ref> <ref>PMID:18164316</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 20:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Arnaudo, N.]]	+	[[Category: Human]]
-	[[Category: Barford, D.]]	+	[[Category: Arnaudo, N]]
-	[[Category: Busch, M.]]	+	[[Category: Barford, D]]
-	[[Category: Carroll, K S.]]	+	[[Category: Busch, M]]
-	[[Category: Garcia, F J.]]	+	[[Category: Carroll, K S]]
-	[[Category: Komander, D.]]	+	[[Category: Garcia, F J]]
-	[[Category: Kulathu, Y.]]	+	[[Category: Komander, D]]
-	[[Category: Mevissen, T E.T.]]	+	[[Category: Kulathu, Y]]
		+	[[Category: Mevissen, T E.T]]
	[[Category: Cys protease]]		[[Category: Cys protease]]
	[[Category: Deubiquitinating enzyme]]		[[Category: Deubiquitinating enzyme]]

OCA at 06:47, 5 November 2014

OCA — Wed, 05 Nov 2014 06:47:41 GMT

←Older revision		Revision as of 06:47, 5 November 2014
Line 1:		Line 1:
-	[[~~Image:~~3zjg.~~jpg~~\|~~left~~\|~~200px~~]]	+	==A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.==
		+	<StructureSection load='3zjg' size='340' side='right' caption='[[3zjg]], [[Resolution\|resolution]] 1.92Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3zjg]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZJG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ZJG FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3zjd\|3zjd]], [[3zje\|3zje]], [[3zjf\|3zjf]]</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=3zjg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zjg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3zjg RCSB], [http://www.ebi.ac.uk/pdbsum/3zjg PDBsum]</span></td></tr>
		+	</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Protein ubiquitination is a highly versatile post-translational modification that regulates as diverse processes as protein degradation and kinase activation. Deubiquitinases hydrolyse ubiquitin modifications from proteins and are hence key regulators of the ubiquitin system. Ovarian tumour deubiquitinases comprise a family of fourteen human enzymes, many of which regulate cellular signalling pathways. Ovarian tumour deubiquitinases are cysteine proteases that cleave polyubiquitin chains in vitro and in cells, but little is currently known about their regulation. Here we show that ovarian tumour deubiquitinases are susceptible to reversible oxidation of the catalytic cysteine residue. High-resolution crystal structures of the catalytic domain of A20 in four different oxidation states reveal that the reversible form of A20 oxidation is a cysteine sulphenic acid intermediate, which is stabilised by the architecture of the catalytic centre. Using chemical tools to detect sulphenic acid intermediates, we show that many ovarian tumour deubiquitinases undergo reversible oxidation upon treatment with HO, revealing a new mechanism to regulate deubiquitinase activity.

-	~~{{STRUCTURE_3zjg\| PDB=3zjg \| SCENE= }}~~	+	Regulation of A20 and other OTU deubiquitinases by reversible oxidation.,Kulathu Y, Garcia FJ, Mevissen TE, Busch M, Arnaudo N, Carroll KS, Barford D, Komander D Nat Commun. 2013 Mar 5;4:1569. doi: 10.1038/ncomms2567. PMID:23463012<ref>PMID:23463012</ref>

-	~~===A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak~~.~~===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-		+	== References ==
-	==~~About this Structure~~==	+	<references/>
-	~~[[3zjg]] is a 2 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=3ZJG OCA].~~	+	__TOC__
-	~~[[Category: Homo sapiens]]~~	+	</StructureSection>
	[[Category: Arnaudo, N.]]		[[Category: Arnaudo, N.]]
	[[Category: Barford, D.]]		[[Category: Barford, D.]]

OCA at 14:21, 6 March 2013

OCA — Wed, 06 Mar 2013 14:21:06 GMT

←Older revision		Revision as of 14:21, 6 March 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3zjg.jpg\|left\|200px]]

-	~~The entry~~ 3zjg ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_3zjg\| PDB=3zjg \| SCENE= }}

-	~~Authors: Kulathu, Y., Garcia, F.J., Mevissen, T.E.T., Busch, M., Arnaudo, N., Carroll, K.S., Barford, D., Komander, D~~.	+	===A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.===

-	~~Description: A20 OTU domain~~ with ~~irreversibly oxidised Cys103~~ from ~~60 min H2O2 soak~~.	+
		+	==About this Structure==
		+	[[3zjg]] is a 2 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=3ZJG OCA].
		+	[[Category: Homo sapiens]]
		+	[[Category: Arnaudo, N.]]
		+	[[Category: Barford, D.]]
		+	[[Category: Busch, M.]]
		+	[[Category: Carroll, K S.]]
		+	[[Category: Garcia, F J.]]
		+	[[Category: Komander, D.]]
		+	[[Category: Kulathu, Y.]]
		+	[[Category: Mevissen, T E.T.]]
		+	[[Category: Cys protease]]
		+	[[Category: Deubiquitinating enzyme]]
		+	[[Category: Hydrolase]]
		+	[[Category: Reversible oxidation]]
		+	[[Category: Sulphenic acid]]
		+	[[Category: Sulphinic acid]]
		+	[[Category: Sulphonic acid]]
		+	[[Category: Ubiquitin]]

OCA at 11:48, 30 January 2013

OCA — Wed, 30 Jan 2013 11:48:24 GMT

←Older revision		Revision as of 11:48, 30 January 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3zjg is ON HOLD	+	The entry 3zjg is ON HOLD until Paper Publication

	Authors: Kulathu, Y., Garcia, F.J., Mevissen, T.E.T., Busch, M., Arnaudo, N., Carroll, K.S., Barford, D., Komander, D.		Authors: Kulathu, Y., Garcia, F.J., Mevissen, T.E.T., Busch, M., Arnaudo, N., Carroll, K.S., Barford, D., Komander, D.

	Description: A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.		Description: A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.

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

OCA — Wed, 23 Jan 2013 10:58:02 GMT

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

←Older revision

Revision as of 10:58, 23 January 2013

OCA: New page: '''Unreleased structure''' The entry 3zjg is ON HOLD Authors: Kulathu, Y., Garcia, F.J., Mevissen, T.E.T., Busch, M., Arnaudo, N., Carroll, K.S., Barford, D., Komander, D. Description:...

OCA — Wed, 23 Jan 2013 10:58:01 GMT

New page: '''Unreleased structure''' The entry 3zjg is ON HOLD Authors: Kulathu, Y., Garcia, F.J., Mevissen, T.E.T., Busch, M., Arnaudo, N., Carroll, K.S., Barford, D., Komander, D. Description:...

New page

'''Unreleased structure'''

The entry 3zjg is ON HOLD

Authors: Kulathu, Y., Garcia, F.J., Mevissen, T.E.T., Busch, M., Arnaudo, N., Carroll, K.S., Barford, D., Komander, D.

Description: A20 OTU domain with irreversibly oxidised Cys103 from 60 min H2O2 soak.