4wph - Revision history

OCA at 00:54, 28 December 2023

OCA — Thu, 28 Dec 2023 00:54:53 GMT

←Older revision		Revision as of 00:54, 28 December 2023
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4wph]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WPH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4wph]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WPH 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]] 2.92Å</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [https://pdbe.org/4wph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [https://www.ebi.ac.uk/pdbsum/4wph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wph 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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [https://pdbe.org/4wph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [https://www.ebi.ac.uk/pdbsum/4wph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wph ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:20, 7 April 2023

OCA — Fri, 07 Apr 2023 07:20:02 GMT

←Older revision		Revision as of 07:20, 7 April 2023
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	<StructureSection load='4wph' size='340' side='right'caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>		<StructureSection load='4wph' size='340' side='right'caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wph]] 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=4WPH OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4WPH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wph]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_1_strain_17 Human alphaherpesvirus 1 strain 17]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4WPH 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wpi\|4wpi]]</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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [https://pdbe.org/4wph PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [https://www.ebi.ac.uk/pdbsum/4wph PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4wph ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">USP7, HAUSP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [~~http~~://pdbe.org/4wph PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4wph PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4wph ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UBP7_HUMAN UBP7_HUMAN]] Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.<ref>PMID:11923872</ref> <ref>PMID:14506283</ref> <ref>PMID:15053880</ref> <ref>PMID:16160161</ref> <ref>PMID:16964248</ref> <ref>PMID:18716620</ref> <ref>PMID:18590780</ref> <ref>PMID:20153724</ref> <ref>PMID:21745816</ref> <ref>PMID:22411829</ref> <ref>PMID:22689415</ref> <ref>PMID:22466611</ref> <ref>PMID:22466612</ref>	+	[https://www.uniprot.org/uniprot/UBP7_HUMAN UBP7_HUMAN] Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.<ref>PMID:11923872</ref> <ref>PMID:14506283</ref> <ref>PMID:15053880</ref> <ref>PMID:16160161</ref> <ref>PMID:16964248</ref> <ref>PMID:18716620</ref> <ref>PMID:18590780</ref> <ref>PMID:20153724</ref> <ref>PMID:21745816</ref> <ref>PMID:22411829</ref> <ref>PMID:22689415</ref> <ref>PMID:22466611</ref> <ref>PMID:22466612</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	==See Also==		==See Also==
-	*[[Thioesterase\|Thioesterase]]	+	*[[Thioesterase 3D structures\|Thioesterase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: Human]]	+	[[Category: Homo sapiens]]
		+	[[Category: Human alphaherpesvirus 1 strain 17]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitinyl hydrolase 1]]~~	+	[[Category: Lacdao I]]
-	[[Category: Lacdao, I]]	+	[[Category: Pfoh R]]
-	[[Category: Pfoh, R]]	+	[[Category: Saridakis V]]
-	[[Category: Saridakis, V]]	+
-	~~[[Category: Hausp]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Icp0 binding site~~]]	+

OCA at 07:50, 8 January 2020

OCA — Wed, 08 Jan 2020 07:50:10 GMT

←Older revision		Revision as of 07:50, 8 January 2020
Line 1:		Line 1:

	==Crystal structure of USP7 ubiquitin-like domains in compact conformation==		==Crystal structure of USP7 ubiquitin-like domains in compact conformation==
-	<StructureSection load='4wph' size='340' side='right' caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>	+	<StructureSection load='4wph' size='340' side='right'caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4wph]] 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=4WPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WPH FirstGlance]. <br>		<table><tr><td colspan='2'>[[4wph]] 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=4WPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WPH FirstGlance]. <br>
Line 21:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4wph" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4wph" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioesterase\|Thioesterase]]
	== References ==		== References ==
	<references/>		<references/>
Line 26:		Line 29:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Lacdao, I]]		[[Category: Lacdao, I]]

OCA at 12:13, 6 November 2017

OCA — Mon, 06 Nov 2017 12:13:08 GMT

←Older revision		Revision as of 12:13, 6 November 2017
Line 3:		Line 3:
	<StructureSection load='4wph' size='340' side='right' caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>		<StructureSection load='4wph' size='340' side='right' caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4wph]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WPH FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4wph]] 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=4WPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WPH 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wpi\|4wpi]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wpi\|4wpi]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">USP7, HAUSP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [http://pdbe.org/4wph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [http://www.ebi.ac.uk/pdbsum/4wph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wph ProSAT]</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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [http://pdbe.org/4wph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [http://www.ebi.ac.uk/pdbsum/4wph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wph ProSAT]</span></td></tr>
Line 20:		Line 21:
	</div>		</div>
	<div class="pdbe-citations 4wph" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4wph" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Thioesterase\|Thioesterase]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Lacdao, I]]		[[Category: Lacdao, I]]

OCA at 17:07, 22 March 2017

OCA — Wed, 22 Mar 2017 17:07:48 GMT

←Older revision		Revision as of 17:07, 22 March 2017
Line 1:		Line 1:
		+
	==Crystal structure of USP7 ubiquitin-like domains in compact conformation==		==Crystal structure of USP7 ubiquitin-like domains in compact conformation==
	<StructureSection load='4wph' size='340' side='right' caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>		<StructureSection load='4wph' size='340' side='right' caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wpi\|4wpi]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wpi\|4wpi]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [http://www.ebi.ac.uk/pdbsum/4wph 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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [http://pdbe.org/4wph PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [http://www.ebi.ac.uk/pdbsum/4wph PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4wph 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 4wph" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Thioesterase\|Thioesterase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 15:13, 17 June 2015

OCA — Wed, 17 Jun 2015 15:13:56 GMT

←Older revision		Revision as of 15:13, 17 June 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of USP7 ubiquitin-like domains in compact conformation==
		+	<StructureSection load='4wph' size='340' side='right' caption='[[4wph]], [[Resolution\|resolution]] 2.92Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4wph]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WPH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WPH 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='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4wpi\|4wpi]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Ubiquitinyl_hydrolase_1 Ubiquitinyl hydrolase 1], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.12 3.4.19.12] </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=4wph FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wph OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wph RCSB], [http://www.ebi.ac.uk/pdbsum/4wph PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UBP7_HUMAN UBP7_HUMAN]] Hydrolase that deubiquitinates target proteins such as FOXO4, p53/TP53, MDM2, ERCC6, DNMT1, UHRF1, PTEN and DAXX. Together with DAXX, prevents MDM2 self-ubiquitination and enhances the E3 ligase activity of MDM2 towards p53/TP53, thereby promoting p53/TP53 ubiquitination and proteasomal degradation. Deubiquitinates p53/TP53 and MDM2 and strongly stabilizes p53/TP53 even in the presence of excess MDM2, and also induces p53/TP53-dependent cell growth repression and apoptosis. Deubiquitination of FOXO4 in presence of hydrogen peroxide is not dependent on p53/TP53 and inhibits FOXO4-induced transcriptional activity. In association with DAXX, is involved in the deubiquitination and translocation of PTEN from the nucleus to the cytoplasm, both processes that are counteracted by PML. Involved in cell proliferation during early embryonic development. Involved in transcription-coupled nucleotide excision repair (TC-NER) in response to UV damage: recruited to DNA damage sites following interaction with KIAA1530/UVSSA and promotes deubiquitination of ERCC6, preventing UV-induced degradation of ERCC6. Contributes to the overall stabilization and trans-activation capability of the herpesvirus 1 trans-acting transcriptional protein ICP0/VMW110 during HSV-1 infection. Involved in maintenance of DNA methylation via its interaction with UHRF1 and DNMT1: acts by mediating deubiquitination of UHRF1 and DNMT1, preventing their degradation and promoting DNA methylation by DNMT1. Exhibits a preference towards 'Lys-48'-linked Ubiquitin chains.<ref>PMID:11923872</ref> <ref>PMID:14506283</ref> <ref>PMID:15053880</ref> <ref>PMID:16160161</ref> <ref>PMID:16964248</ref> <ref>PMID:18716620</ref> <ref>PMID:18590780</ref> <ref>PMID:20153724</ref> <ref>PMID:21745816</ref> <ref>PMID:22411829</ref> <ref>PMID:22689415</ref> <ref>PMID:22466611</ref> <ref>PMID:22466612</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Herpes simplex virus-1 immediate-early protein ICP0 activates viral genes during early stages of infection, affects cellular levels of multiple host proteins and is crucial for effective lytic infection. Being a RING-type E3 ligase prone to auto-ubiquitination, ICP0 relies on human deubiquitinating enzyme USP7 for protection against 26S proteasomal mediated degradation. USP7 is involved in apoptosis, epigenetics, cell proliferation and is targeted by several herpesviruses. Several USP7 partners, including ICP0, GMPS, and UHRF1, interact through its C-terminal domain (CTD), which contains five ubiquitin-like (Ubl) structures. Despite the fact that USP7 has emerged as a drug target for cancer therapy, structural details of USP7 regulation and the molecular mechanism of interaction at its CTD have remained elusive. Here, we mapped the binding site between an ICP0 peptide and USP7 and determined the crystal structure of the first three Ubl domains bound to the ICP0 peptide, which showed that ICP0 binds to a loop on Ubl2. Sequences similar to the USP7-binding site in ICP0 were identified in GMPS and UHRF1 and shown to bind USP7-CTD through Ubl2. In addition, co-immunoprecipitation assays in human cells comparing binding to USP7 with and without a Ubl2 mutation, confirmed the importance of the Ubl2 binding pocket for binding ICP0, GMPS and UHRF1. Therefore we have identified a novel mechanism of USP7 recognition that is used by both viral and cellular proteins. Our structural information was used to generate a model of near full-length USP7, showing the relative position of the ICP0/GMPS/UHRF1 binding pocket and the structural basis by which it could regulate enzymatic activity.

-	~~The entry 4wph is ON HOLD until Paper Publication~~	+	Crystal Structure of USP7 Ubiquitin-like Domains with an ICP0 Peptide Reveals a Novel Mechanism Used by Viral and Cellular Proteins to Target USP7.,Pfoh R, Lacdao IK, Georges AA, Capar A, Zheng H, Frappier L, Saridakis V PLoS Pathog. 2015 Jun 5;11(6):e1004950. doi: 10.1371/journal.ppat.1004950., eCollection 2015 Jun. PMID:26046769<ref>PMID:26046769</ref>

-	~~Authors: Pfoh~~, R.~~, Lacdao, I~~.~~, Saridakis, V~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description:~~	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Lacdao, I]]		[[Category: Lacdao, I]]
		+	[[Category: Pfoh, R]]
	[[Category: Saridakis, V]]		[[Category: Saridakis, V]]
-	[[Category: ~~Pfoh, R~~]]	+	[[Category: Hausp]]
		+	[[Category: Hydrolase]]
		+	[[Category: Icp0 binding site]]

OCA at 19:49, 24 December 2014

OCA — Wed, 24 Dec 2014 19:49:43 GMT

←Older revision		Revision as of 19:49, 24 December 2014
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	Authors: Pfoh, R., Lacdao, I., Saridakis, V.		Authors: Pfoh, R., Lacdao, I., Saridakis, V.

-	Description:	+	Description:
		+	[[Category: Unreleased Structures]]
		+	[[Category: Lacdao, I]]
		+	[[Category: Saridakis, V]]
		+	[[Category: Pfoh, R]]

OCA at 11:54, 19 November 2014

OCA — Wed, 19 Nov 2014 11:54:48 GMT

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	Authors: Pfoh, R., Lacdao, I., Saridakis, V.		Authors: Pfoh, R., Lacdao, I., Saridakis, V.

	Description:		Description:

OCA: Protected "4wph" [edit=sysop:move=sysop]

OCA — Wed, 29 Oct 2014 10:33:57 GMT

Protected "4wph" [edit=sysop:move=sysop]

←Older revision

Revision as of 10:33, 29 October 2014

OCA: New page: '''Unreleased structure''' The entry 4wph is ON HOLD Authors: Pfoh, R., Lacdao, I., Saridakis, V. Description:

OCA — Wed, 29 Oct 2014 10:33:55 GMT

New page: '''Unreleased structure''' The entry 4wph is ON HOLD Authors: Pfoh, R., Lacdao, I., Saridakis, V. Description:

New page

'''Unreleased structure'''

The entry 4wph is ON HOLD

Authors: Pfoh, R., Lacdao, I., Saridakis, V.

Description: