4mel - Revision history

OCA at 16:36, 20 September 2023

2023-09-20T16:36:32Z

←Older revision		Revision as of 16:36, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4mel]] 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=4MEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MEL FirstGlance]. <br>		<table><tr><td colspan='2'>[[4mel]] 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=4MEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MEL FirstGlance]. <br>
-	</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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [https://pdbe.org/4mel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [https://www.ebi.ac.uk/pdbsum/4mel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mel ProSAT]</span></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]] 2.899Å</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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [https://pdbe.org/4mel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [https://www.ebi.ac.uk/pdbsum/4mel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mel ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 11:12, 21 December 2022

2022-12-21T11:12:28Z

←Older revision		Revision as of 11:12, 21 December 2022
Line 3:		Line 3:
	<StructureSection load='4mel' size='340' side='right'caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4mel' size='340' side='right'caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4mel]] 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=4MEL OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4MEL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4mel]] 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=4MEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4MEL FirstGlance]. <br>
-	</td></tr>~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>~~	+	</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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [https://pdbe.org/4mel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [https://www.ebi.ac.uk/pdbsum/4mel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mel ProSAT]</span></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UHX1, USP11 ([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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [~~http~~://pdbe.org/4mel PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4mel PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4mel ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/UBP11_HUMAN UBP11_HUMAN]] Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks.<ref>PMID:15314155</ref> <ref>PMID:17897950</ref> <ref>PMID:18408009</ref> <ref>PMID:19874889</ref> <ref>PMID:20233726</ref>	+	[https://www.uniprot.org/uniprot/UBP11_HUMAN UBP11_HUMAN] Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks.<ref>PMID:15314155</ref> <ref>PMID:17897950</ref> <ref>PMID:18408009</ref> <ref>PMID:19874889</ref> <ref>PMID:20233726</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 19:

	==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: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Ubiquitinyl hydrolase 1]]~~	+	[[Category: Cornaciu I]]
-	[[Category: Cornaciu, I]]	+	[[Category: Dreveny I]]
-	[[Category: Dreveny, I]]	+	[[Category: Emsley J]]
-	[[Category: Emsley, J]]	+	[[Category: Gratton HE]]
-	[[Category: Gratton~~, H E~~]]	+	[[Category: Harper S]]
-	[[Category: Harper, S]]	+	[[Category: Oberer M]]
-	[[Category: Oberer, M]]	+	[[Category: Scott DJ]]
-	[[Category: Scott~~, D J]]~~	+
-	~~[[Category: Deubiquitinating enzyme]]~~	+
-	~~[[Category: Du finger]]~~	+
-	~~[[Category: Dub]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Ubiquitin thiolesterase~~]]	+

OCA at 09:10, 10 April 2019

2019-04-10T09:10:55Z

←Older revision		Revision as of 09:10, 10 April 2019
Line 1:		Line 1:

	==Crystal Structure of the human USP11 DUSP-UBL domains==		==Crystal Structure of the human USP11 DUSP-UBL domains==
-	<StructureSection load='4mel' size='340' side='right' caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>	+	<StructureSection load='4mel' size='340' side='right'caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4mel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEL FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4mel]] 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=4MEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEL FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">UHX1, USP11 ([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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://pdbe.org/4mel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mel 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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://pdbe.org/4mel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mel ProSAT]</span></td></tr>
Line 26:		Line 27:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
	[[Category: Cornaciu, I]]		[[Category: Cornaciu, I]]

OCA at 20:02, 4 August 2016

2016-08-04T20:02:51Z

←Older revision		Revision as of 20:02, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of the human USP11 DUSP-UBL domains==		==Crystal Structure of the human USP11 DUSP-UBL domains==
	<StructureSection load='4mel' size='340' side='right' caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4mel' size='340' side='right' caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel 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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://pdbe.org/4mel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4mel ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4mel" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 12:40, 25 December 2014

2014-12-25T12:40:22Z

←Older revision		Revision as of 12:40, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4mel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEL FirstGlance]. <br>		<table><tr><td colspan='2'>[[4mel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEL FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>
-	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel 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=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/UBP11_HUMAN UBP11_HUMAN]] Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks.<ref>PMID:15314155</ref> <ref>PMID:17897950</ref> <ref>PMID:18408009</ref> <ref>PMID:19874889</ref> <ref>PMID:20233726</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 13:		Line 15:
	Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains.,Harper S, Gratton HE, Cornaciu I, Oberer M, Scott DJ, Emsley J, Dreveny I Biochemistry. 2014 Apr 29. PMID:24724799<ref>PMID:24724799</ref>		Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains.,Harper S, Gratton HE, Cornaciu I, Oberer M, Scott DJ, Emsley J, Dreveny I Biochemistry. 2014 Apr 29. PMID:24724799<ref>PMID:24724799</ref>

-	From ~~MEDLINEÂ®~~/~~PubMedÂ®~~, 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>
		+
		+	==See Also==
		+	*[[Thioesterase\|Thioesterase]]
	== References ==		== References ==
	<references/>		<references/>
Line 20:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Ubiquitinyl hydrolase 1]]		[[Category: Ubiquitinyl hydrolase 1]]
-	[[Category: Cornaciu, I.]]	+	[[Category: Cornaciu, I]]
-	[[Category: Dreveny, I.]]	+	[[Category: Dreveny, I]]
-	[[Category: Emsley, J.]]	+	[[Category: Emsley, J]]
-	[[Category: Gratton, H E.]]	+	[[Category: Gratton, H E]]
-	[[Category: Harper, S.]]	+	[[Category: Harper, S]]
-	[[Category: Oberer, M.]]	+	[[Category: Oberer, M]]
-	[[Category: Scott, D J.]]	+	[[Category: Scott, D J]]
	[[Category: Deubiquitinating enzyme]]		[[Category: Deubiquitinating enzyme]]
	[[Category: Du finger]]		[[Category: Du finger]]

OCA at 07:19, 28 May 2014

2014-05-28T07:19:25Z

←Older revision		Revision as of 07:19, 28 May 2014
Line 2:		Line 2:
	<StructureSection load='4mel' size='340' side='right' caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>		<StructureSection load='4mel' size='340' side='right' caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4mel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEL OCA]. <br>	+	<table><tr><td colspan='2'>[[4mel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MEL FirstGlance]. <br>
	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>		</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/~~Glucokinase Glucokinase~~], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.~~2 2~~.7.1.2] </span></td></tr>	+	<tr><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><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel PDBsum]</span></td></tr>		<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel PDBsum]</span></td></tr>
	<table>		<table>

OCA at 08:15, 7 May 2014

2014-05-07T08:15:57Z

←Older revision		Revision as of 08:15, 7 May 2014
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal Structure of the human USP11 DUSP-UBL domains==
		+	<StructureSection load='4mel' size='340' side='right' caption='[[4mel]], [[Resolution\|resolution]] 2.90Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4mel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MEL OCA]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4mem\|4mem]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mel OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mel RCSB], [http://www.ebi.ac.uk/pdbsum/4mel PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The ubiquitin specific protease 11 (USP11) is implicated in DNA repair, viral RNA replication, and TGFbeta signaling. We report the first characterization of the USP11 domain architecture and its role in regulating the enzymatic activity. USP11 consists of an N-terminal "domain present in USPs" (DUSP) and "ubiquitin-like" (UBL) domain, together referred to as DU domains, and the catalytic domain harboring a second UBL domain. Crystal structures of the DU domains show a tandem arrangement with a shortened beta-hairpin at the two-domain interface and altered surface characteristics compared to the homologues USP4 and USP15. A conserved VEVY motif is a signature feature at the two-domain interface that shapes a potential protein interaction site. Small angle X-ray scattering and gel filtration experiments are consistent with the USP11DU domains and full-length USP11 being monomeric. Unexpectedly, we reveal, through kinetic assays of a series of deletion mutants, that the catalytic activity of USP11 is not regulated through intramolecular autoinhibition or activation by the N-terminal DU or UBL domains. Moreover, ubiquitin chain cleavage assays with all eight linkages reveal a preference for Lys63-, Lys6-, Lys33-, and Lys11-linked chains over Lys27-, Lys29-, and Lys48-linked and linear chains consistent with USP11's function in DNA repair pathways that is mediated by the protease domain. Our data support a model whereby USP11 domains outside the catalytic core domain serve as protein interaction or trafficking modules rather than a direct regulatory function of the proteolytic activity. This highlights the diversity of USPs in substrate recognition and regulation of ubiquitin deconjugation.

-	~~The entry 4mel is ON HOLD until Paper Publication~~	+	Structure and Catalytic Regulatory Function of Ubiquitin Specific Protease 11 N-Terminal and Ubiquitin-like Domains.,Harper S, Gratton HE, Cornaciu I, Oberer M, Scott DJ, Emsley J, Dreveny I Biochemistry. 2014 Apr 29. PMID:24724799<ref>PMID:24724799</ref>

-	~~Authors: Harper~~, S., Gratton, H.E., ~~Cornaciu, I~~., Oberer, M., Scott, D.J.~~, Emsley, J., Dreveny, I.~~	+	From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description~~: ~~Crystal Structure of the human USP11 DUSP-UBL domains~~	+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Ubiquitinyl hydrolase 1]]
		+	[[Category: Cornaciu, I.]]
		+	[[Category: Dreveny, I.]]
		+	[[Category: Emsley, J.]]
		+	[[Category: Gratton, H E.]]
		+	[[Category: Harper, S.]]
		+	[[Category: Oberer, M.]]
		+	[[Category: Scott, D J.]]
		+	[[Category: Deubiquitinating enzyme]]
		+	[[Category: Du finger]]
		+	[[Category: Dub]]
		+	[[Category: Hydrolase]]
		+	[[Category: Ubiquitin thiolesterase]]

OCA at 03:37, 20 September 2013

2013-09-20T03:37:33Z

←Older revision		Revision as of 03:37, 20 September 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4mel is ON HOLD	+	The entry 4mel is ON HOLD until Paper Publication

-	Authors: Harper, S., Gratton, H.E., Oberer, M., Scott, D.J., Emsley, J., Dreveny, I.	+	Authors: Harper, S., Gratton, H.E., Cornaciu, I., Oberer, M., Scott, D.J., Emsley, J., Dreveny, I.

	Description: Crystal Structure of the human USP11 DUSP-UBL domains		Description: Crystal Structure of the human USP11 DUSP-UBL domains

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

2013-09-04T10:03:40Z

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

←Older revision

Revision as of 10:03, 4 September 2013

OCA: New page: '''Unreleased structure''' The entry 4mel is ON HOLD Authors: Harper, S., Gratton, H.E., Oberer, M., Scott, D.J., Emsley, J., Dreveny, I. Description: Crystal Structure of the human US...

2013-09-04T10:03:39Z

New page: '''Unreleased structure''' The entry 4mel is ON HOLD Authors: Harper, S., Gratton, H.E., Oberer, M., Scott, D.J., Emsley, J., Dreveny, I. Description: Crystal Structure of the human US...

New page

'''Unreleased structure'''

The entry 4mel is ON HOLD

Authors: Harper, S., Gratton, H.E., Oberer, M., Scott, D.J., Emsley, J., Dreveny, I.

Description: Crystal Structure of the human USP11 DUSP-UBL domains