4n6n - Revision history

OCA at 16:48, 20 September 2023

OCA — Wed, 20 Sep 2023 16:48:44 GMT

←Older revision		Revision as of 16:48, 20 September 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4n6n]] 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=4N6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N6N FirstGlance]. <br>		<table><tr><td colspan='2'>[[4n6n]] 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=4N6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N6N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</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]] 1.87Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [https://pdbe.org/4n6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [https://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n 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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [https://pdbe.org/4n6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [https://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n ProSAT]</span></td></tr>
	</table>		</table>

OCA at 08:12, 11 January 2023

OCA — Wed, 11 Jan 2023 08:12:15 GMT

←Older revision		Revision as of 08:12, 11 January 2023
Line 3:		Line 3:
	<StructureSection load='4n6n' size='340' side='right'caption='[[4n6n]], [[Resolution\|resolution]] 1.87Å' scene=''>		<StructureSection load='4n6n' size='340' side='right'caption='[[4n6n]], [[Resolution\|resolution]] 1.87Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4n6n]] 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=4N6N OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4N6N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4n6n]] 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=4N6N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N6N FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr>
-	~~<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [https://pdbe.org/4n6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [https://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n ProSAT]</span></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n6l\|4n6l]], [[4n6m\|4n6m]], [[4n6o\|4n6o]]</td></tr>~~	+
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LGMN, PRSC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CST6 ([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/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [~~http~~://pdbe.org/4n6n PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/LGMN_HUMAN LGMN_HUMAN]] Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system~~. [[http://www.uniprot.org/uniprot/CYTM_HUMAN CYTM_HUMAN]] Shows moderate inhibition of cathepsin B but is not active against cathepsin C~~.	+	[https://www.uniprot.org/uniprot/LGMN_HUMAN LGMN_HUMAN] Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 26:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	~~[[Category: Legumain]]~~	+	[[Category: Brandstetter H]]
-	[[Category: Brandstetter, H]]	+	[[Category: Dall E]]
-	[[Category: Dall, E]]	+
-	~~[[Category: Asparaginyl endopeptidase]]~~	+
-	~~[[Category: Cancer]]~~	+
-	~~[[Category: Cathepsin]]~~	+
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Cysteine protease]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Inhibitor]]~~	+
-	~~[[Category: Papain]]~~	+
-	~~[[Category: Reactive center loop~~]]	+

OCA at 08:46, 10 April 2019

OCA — Wed, 10 Apr 2019 08:46:57 GMT

←Older revision		Revision as of 08:46, 10 April 2019
Line 1:		Line 1:

	==Crystal structure of oxidized legumain in complex with cystatin E/M==		==Crystal structure of oxidized legumain in complex with cystatin E/M==
-	<StructureSection load='4n6n' size='340' side='right' caption='[[4n6n]], [[Resolution\|resolution]] 1.87Å' scene=''>	+	<StructureSection load='4n6n' size='340' side='right'caption='[[4n6n]], [[Resolution\|resolution]] 1.87Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4n6n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N6N FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4n6n]] 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=4N6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N6N FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr>		<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n6l\|4n6l]], [[4n6m\|4n6m]], [[4n6o\|4n6o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n6l\|4n6l]], [[4n6m\|4n6m]], [[4n6o\|4n6o]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">LGMN, PRSC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), CST6 ([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/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [http://pdbe.org/4n6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [http://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n 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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [http://pdbe.org/4n6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [http://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n ProSAT]</span></td></tr>
Line 25:		Line 26:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Legumain]]		[[Category: Legumain]]
	[[Category: Brandstetter, H]]		[[Category: Brandstetter, H]]

OCA at 07:17, 23 December 2016

OCA — Fri, 23 Dec 2016 07:17:21 GMT

←Older revision		Revision as of 07:17, 23 December 2016
Line 1:		Line 1:
		+
	==Crystal structure of oxidized legumain in complex with cystatin E/M==		==Crystal structure of oxidized legumain in complex with cystatin E/M==
	<StructureSection load='4n6n' size='340' side='right' caption='[[4n6n]], [[Resolution\|resolution]] 1.87Å' scene=''>		<StructureSection load='4n6n' size='340' side='right' caption='[[4n6n]], [[Resolution\|resolution]] 1.87Å' scene=''>
Line 7:		Line 8:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n6l\|4n6l]], [[4n6m\|4n6m]], [[4n6o\|4n6o]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n6l\|4n6l]], [[4n6m\|4n6m]], [[4n6o\|4n6o]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [http://www.ebi.ac.uk/pdbsum/4n6n 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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [http://pdbe.org/4n6n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [http://www.ebi.ac.uk/pdbsum/4n6n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n6n ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 19:		Line 20:
	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 4n6n" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 12:59, 18 February 2015

OCA — Wed, 18 Feb 2015 12:59:35 GMT

←Older revision		Revision as of 12:59, 18 February 2015
Line 1:		Line 1:
-	'''~~Unreleased~~ structure'''	+	==Crystal structure of oxidized legumain in complex with cystatin E/M==
		+	<StructureSection load='4n6n' size='340' side='right' caption='[[4n6n]], [[Resolution\|resolution]] 1.87Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4n6n]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4N6N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N6N FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=IOD:IODIDE+ION'>IOD</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
		+	<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue\|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SCH:S-METHYL-THIO-CYSTEINE'>SCH</scene>, <scene name='pdbligand=SNN:L-3-AMINOSUCCINIMIDE'>SNN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[4n6l\|4n6l]], [[4n6m\|4n6m]], [[4n6o\|4n6o]]</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Legumain Legumain], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.34 3.4.22.34] </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=4n6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n6n OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4n6n RCSB], [http://www.ebi.ac.uk/pdbsum/4n6n PDBsum]</span></td></tr>
		+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/LGMN_HUMAN LGMN_HUMAN]] Has a strict specificity for hydrolysis of asparaginyl bonds. Can also cleave aspartyl bonds slowly, especially under acidic conditions. May be involved in the processing of proteins for MHC class II antigen presentation in the lysosomal/endosomal system. [[http://www.uniprot.org/uniprot/CYTM_HUMAN CYTM_HUMAN]] Shows moderate inhibition of cathepsin B but is not active against cathepsin C.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Peptide ligases expand the repertoire of genetically encoded protein architectures by synthesizing new peptide bonds, energetically driven by ATP or NTPs. Here, we report the discovery of a genuine ligase activity in human legumain (AEP) which has important roles in immunity and tumor progression that were believed to be due to its established cysteine protease activity. Defying dogma, the ligase reaction is independent of the catalytic cysteine but exploits an endogenous energy reservoir that results from the conversion of a conserved aspartate to a metastable aspartimide. Legumain's dual protease-ligase activities are pH- and thus localization controlled, dominating at acidic and neutral pH, respectively. Their relevance includes reversible on-off switching of cystatin inhibitors and enzyme (in)activation, and may affect the generation of three-dimensional MHC epitopes. The aspartate-aspartimide (succinimide) pair represents a new paradigm of coupling endergonic reactions in ATP-scarce environments.

-	~~The entry 4n6n is ON HOLD until Mar 14 2016~~	+	Structure and Mechanism of an Aspartimide-Dependent Peptide Ligase in Human Legumain.,Dall E, Fegg JC, Briza P, Brandstetter H Angew Chem Int Ed Engl. 2015 Jan 28. doi: 10.1002/anie.201409135. PMID:25630877<ref>PMID:25630877</ref>

-	~~Authors: Dall~~, E.~~, Brandstetter, H~~.	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~Description: Crystal structure of oxidized legumain in complex with cystatin E~~/M	+	== References ==
-	[[Category: ~~Unreleased Structures~~]]	+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Legumain]]
		+	[[Category: Brandstetter, H]]
	[[Category: Dall, E]]		[[Category: Dall, E]]
-	[[Category: ~~Brandstetter, H~~]]	+	[[Category: Asparaginyl endopeptidase]]
		+	[[Category: Cancer]]
		+	[[Category: Cathepsin]]
		+	[[Category: Complex]]
		+	[[Category: Cysteine protease]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Inhibitor]]
		+	[[Category: Papain]]
		+	[[Category: Reactive center loop]]

OCA at 14:11, 24 December 2014

OCA — Wed, 24 Dec 2014 14:11:07 GMT

←Older revision		Revision as of 14:11, 24 December 2014
Line 6:		Line 6:

	Description: Crystal structure of oxidized legumain in complex with cystatin E/M		Description: Crystal structure of oxidized legumain in complex with cystatin E/M
		+	[[Category: Unreleased Structures]]
		+	[[Category: Dall, E]]
		+	[[Category: Brandstetter, H]]

OCA at 10:50, 17 December 2014

OCA — Wed, 17 Dec 2014 10:50:06 GMT

←Older revision		Revision as of 10:50, 17 December 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4n6n is ON HOLD until ~~Jan~~ 14 2016	+	The entry 4n6n is ON HOLD until Mar 14 2016

	Authors: Dall, E., Brandstetter, H.		Authors: Dall, E., Brandstetter, H.

	Description: Crystal structure of oxidized legumain in complex with cystatin E/M		Description: Crystal structure of oxidized legumain in complex with cystatin E/M

OCA at 03:44, 4 September 2014

OCA — Thu, 04 Sep 2014 03:44:18 GMT

←Older revision		Revision as of 03:44, 4 September 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4n6n is ON HOLD until ~~Paper Publication~~	+	The entry 4n6n is ON HOLD until Jan 14 2016

	Authors: Dall, E., Brandstetter, H.		Authors: Dall, E., Brandstetter, H.

	Description: Crystal structure of oxidized legumain in complex with cystatin E/M		Description: Crystal structure of oxidized legumain in complex with cystatin E/M

OCA at 09:38, 16 July 2014

OCA — Wed, 16 Jul 2014 09:38:02 GMT

←Older revision		Revision as of 09:38, 16 July 2014
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4n6n is ON HOLD	+	The entry 4n6n is ON HOLD until Paper Publication

	Authors: Dall, E., Brandstetter, H.		Authors: Dall, E., Brandstetter, H.

	Description: Crystal structure of oxidized legumain in complex with cystatin E/M		Description: Crystal structure of oxidized legumain in complex with cystatin E/M

OCA: Protected "4n6n" [edit=sysop:move=sysop]

OCA — Wed, 23 Oct 2013 06:16:06 GMT

Protected "4n6n" [edit=sysop:move=sysop]

←Older revision

Revision as of 06:16, 23 October 2013