3ofi - Revision history

OCA at 09:37, 6 September 2023

OCA — Wed, 06 Sep 2023 09:37:56 GMT

←Older revision		Revision as of 09:37, 6 September 2023
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	==Crystal structure of human insulin-degrading enzyme in complex with ubiquitin==		==Crystal structure of human insulin-degrading enzyme in complex with ubiquitin==
-	<StructureSection load='3ofi' size='340' side='right' caption='[[3ofi]], [[Resolution\|resolution]] 2.35Å' scene=''>	+	<StructureSection load='3ofi' size='340' side='right'caption='[[3ofi]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ofi]] 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=3OFI OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3OFI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ofi]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OFI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3OFI FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat">~~<scene name='pdbligand=DIO:1,4~~-~~DIETHYLENE+DIOXIDE'>DIO</scene>~~, ~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>~~</td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.35Å</td></tr>
-	<tr id='~~gene~~'><td class="sblockLbl"><b>[[~~Gene~~\|~~Gene~~:]]</b></td><td class="sblockDat"~~>IDE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN])</td~~><~~/tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id~~='~~activity'><td class~~=~~"sblockLbl"><b>Activity~~:~~</b~~></td><~~td class~~=~~"sblockDat"><span class~~=~~'plainlinks~~'>~~[http://en.wikipedia.org/wiki/Insulysin Insulysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.56 3.4.24.56]~~ </~~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=3ofi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofi OCA], [https://pdbe.org/3ofi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ofi RCSB], [https://www.ebi.ac.uk/pdbsum/3ofi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ofi 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=3ofi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofi OCA], [~~http~~://pdbe.org/3ofi PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3ofi RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3ofi PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3ofi ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/IDE_HUMAN IDE_HUMAN]] Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.<ref>PMID:10684867</ref> <ref>PMID:17613531</ref> <ref>PMID:18986166</ref> [[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>	+	[https://www.uniprot.org/uniprot/IDE_HUMAN IDE_HUMAN] Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.<ref>PMID:10684867</ref> <ref>PMID:17613531</ref> <ref>PMID:18986166</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/of/3ofi_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/of/3ofi_consurf.spt"</scriptWhenChecked>
	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>		<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
Line 30:		Line 29:
	</div>		</div>
	<div class="pdbe-citations 3ofi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ofi" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Insulin-degrading enzyme 3D structures\|Insulin-degrading enzyme 3D structures]]
		+	*[[3D structures of ubiquitin\|3D structures of ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Insulysin~~]]	+	[[Category: Large Structures]]
-	[[Category: Kalas, V]]	+	[[Category: Kalas V]]
-	[[Category: Ralat~~, L A~~]]	+	[[Category: Ralat LA]]
-	[[Category: Tang, W J]]	+	[[Category: Tang W-J]]
-	~~[[Category: Exosite]]~~	+
-	~~[[Category: Human insulin-degrading enzyme]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Protein-peptide complex]]~~	+
-	~~[[Category: Ubiquitin~~]]	+

OCA at 08:44, 8 November 2017

OCA — Wed, 08 Nov 2017 08:44:33 GMT

←Older revision		Revision as of 08:44, 8 November 2017
Line 30:		Line 30:
	</div>		</div>
	<div class="pdbe-citations 3ofi" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3ofi" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]
-	*[[Ubiquitin\|Ubiquitin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 09:46, 4 August 2016

OCA — Thu, 04 Aug 2016 09:46:55 GMT

←Older revision		Revision as of 09:46, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal structure of human insulin-degrading enzyme in complex with ubiquitin==		==Crystal structure of human insulin-degrading enzyme in complex with ubiquitin==
	<StructureSection load='3ofi' size='340' side='right' caption='[[3ofi]], [[Resolution\|resolution]] 2.35Å' scene=''>		<StructureSection load='3ofi' size='340' side='right' caption='[[3ofi]], [[Resolution\|resolution]] 2.35Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3ofi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OFI FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3ofi]] 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=3OFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OFI FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">IDE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 ~~Homo sapiens~~])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">IDE ([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/Insulysin Insulysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.56 3.4.24.56] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Insulysin Insulysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.56 3.4.24.56] </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=3ofi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ofi RCSB], [http://www.ebi.ac.uk/pdbsum/3ofi 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=3ofi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofi OCA], [http://pdbe.org/3ofi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ofi RCSB], [http://www.ebi.ac.uk/pdbsum/3ofi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ofi ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 18:		Line 19:
	<text>to colour the structure by Evolutionary Conservation</text>		<text>to colour the structure by Evolutionary Conservation</text>
	</jmolCheckbox>		</jmolCheckbox>
-	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/~~chain_selection~~.php?pdb_ID=~~2ata~~ ConSurf].	+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3ofi ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 28:		Line 29:
	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 3ofi" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 36:		Line 38:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
	[[Category: Kalas, V]]		[[Category: Kalas, V]]

OCA at 08:30, 24 December 2014

OCA — Wed, 24 Dec 2014 08:30:29 GMT

←Older revision		Revision as of 08:30, 24 December 2014
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=3ofi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ofi RCSB], [http://www.ebi.ac.uk/pdbsum/3ofi 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=3ofi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ofi RCSB], [http://www.ebi.ac.uk/pdbsum/3ofi PDBsum]</span></td></tr>
	</table>		</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/IDE_HUMAN IDE_HUMAN]] Plays a role in the cellular breakdown of insulin, IAPP, glucagon, bradykinin, kallidin and other peptides, and thereby plays a role in intercellular peptide signaling. Degrades amyloid formed by APP and IAPP. May play a role in the degradation and clearance of naturally secreted amyloid beta-protein by neurons and microglia.<ref>PMID:10684867</ref> <ref>PMID:17613531</ref> <ref>PMID:18986166</ref> [[http://www.uniprot.org/uniprot/UBC_HUMAN UBC_HUMAN]] Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.<ref>PMID:16543144</ref> <ref>PMID:19754430</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]

OCA at 10:42, 9 December 2014

OCA — Tue, 09 Dec 2014 10:42:13 GMT

←Older revision		Revision as of 10:42, 9 December 2014
Line 1:		Line 1:
-	[[~~Image:~~3ofi.~~png~~\|~~left~~\|200px]]	+	==Crystal structure of human insulin-degrading enzyme in complex with ubiquitin==
		+	<StructureSection load='3ofi' size='340' side='right' caption='[[3ofi]], [[Resolution\|resolution]] 2.35Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3ofi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OFI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3OFI FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DIO:1,4-DIETHYLENE+DIOXIDE'>DIO</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">IDE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Insulysin Insulysin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.56 3.4.24.56] </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=3ofi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ofi OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ofi RCSB], [http://www.ebi.ac.uk/pdbsum/3ofi PDBsum]</span></td></tr>
		+	</table>
		+	== Evolutionary Conservation ==
		+	[[Image:Consurf_key_small.gif\|200px\|right]]
		+	Check<jmol>
		+	<jmolCheckbox>
		+	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/of/3ofi_consurf.spt"</scriptWhenChecked>
		+	<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
		+	<text>to colour the structure by Evolutionary Conservation</text>
		+	</jmolCheckbox>
		+	</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary\|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
		+	<div style="clear:both"></div>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Insulin-degrading enzyme (IDE) can degrade insulin and amyloid-beta, peptides involved in diabetes and Alzheimer's disease, respectively. IDE selects its substrates based on size, charge, and flexibility. From these criteria, we predict that IDE can cleave and inactivate ubiquitin (Ub). Here, we show that IDE cleaves Ub in a biphasic manner, first, by rapidly removing the two C-terminal glycines (k(cat)=2 s(-1)) followed by a slow cleavage between residues 72 and 73 (k(cat)=0.07 s(-1)), thereby producing the inactive 1-74 fragment of Ub (Ub1-74) and 1-72 fragment of Ub (Ub1-72). IDE is a ubiquitously expressed cytosolic protein, where monomeric Ub is also present. Thus, Ub degradation by IDE should be regulated. IDE is known to bind the cytoplasmic intermediate filament protein nestin with high affinity. We found that nestin potently inhibits the cleavage of Ub by IDE. In addition, Ub1-72 has a markedly increased affinity for IDE ( approximately 90-fold). Thus, the association of IDE with cellular regulators and product inhibition by Ub1-72 can prevent inadvertent proteolysis of cellular Ub by IDE. Ub is a highly stable protein. However, IDE instead prefers to degrade peptides with high intrinsic flexibility. Indeed, we demonstrate that IDE is exquisitely sensitive to Ub stability. Mutations that only mildly destabilize Ub (DeltaDeltaG<0.6 kcal/mol) render IDE hypersensitive to Ub with rate enhancements greater than 12-fold. The Ub-bound IDE structure and IDE mutants reveal that the interaction of the exosite with the N-terminus of Ub guides the unfolding of Ub, allowing its sequential cleavages. Together, our studies link the control of Ub clearance with IDE.

-	~~{{STRUCTURE_3ofi\| PDB=3ofi \| SCENE= }}~~	+	Ubiquitin is a novel substrate for human insulin-degrading enzyme.,Ralat LA, Kalas V, Zheng Z, Goldman RD, Sosnick TR, Tang WJ J Mol Biol. 2011 Feb 25;406(3):454-66. Epub 2010 Dec 23. PMID:21185309<ref>PMID:21185309</ref>

-	~~===Crystal structure~~ of ~~human insulin-degrading enzyme in complex with ubiquitin===~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-		+	</div>
-	~~{{ABSTRACT_PUBMED_21185309}}~~	+
-		+
-	~~==About this Structure==~~	+
-	~~[[3ofi]] is a 4 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Homo_sapiens Homo sapiens]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=3OFI OCA].~~	+

	==See Also==		==See Also==
	*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]		*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]
	*[[Ubiquitin\|Ubiquitin]]		*[[Ubiquitin\|Ubiquitin]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<~~ref group="xtra">PMID:021185309<~~/~~ref~~><~~references group="xtra"~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
-	[[Category: Kalas, V.]]	+	[[Category: Kalas, V]]
-	[[Category: Ralat, L A.]]	+	[[Category: Ralat, L A]]
-	[[Category: Tang, W J.]]	+	[[Category: Tang, W J]]
	[[Category: Exosite]]		[[Category: Exosite]]
	[[Category: Human insulin-degrading enzyme]]		[[Category: Human insulin-degrading enzyme]]

OCA at 05:48, 20 October 2012

OCA — Sat, 20 Oct 2012 05:48:14 GMT

←Older revision		Revision as of 05:48, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3ofi]] is a 4 chain structure ~~of [[Insulin-Degrading Enzyme]] and [[Ubiquitin]]~~ 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=3OFI OCA].	+	[[3ofi]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3OFI OCA].

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

OCA at 11:10, 25 July 2012

OCA — Wed, 25 Jul 2012 11:10:40 GMT

←Older revision		Revision as of 11:10, 25 July 2012
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	[[Image:3ofi.png\|left\|200px]]		[[Image:3ofi.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3ofi", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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	{{STRUCTURE_3ofi\| PDB=3ofi \| SCENE= }}		{{STRUCTURE_3ofi\| PDB=3ofi \| SCENE= }}

	===Crystal structure of human insulin-degrading enzyme in complex with ubiquitin===		===Crystal structure of human insulin-degrading enzyme in complex with ubiquitin===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_21185309}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 21185309 is the PubMed ID number.
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	{{ABSTRACT_PUBMED_21185309}}		{{ABSTRACT_PUBMED_21185309}}

	==About this Structure==		==About this Structure==
-	[[3ofi]] is a 4 chain structure of [[Ubiquitin]] 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=3OFI OCA].	+	[[3ofi]] is a 4 chain structure of [[Insulin-Degrading Enzyme]] and [[Ubiquitin]] 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=3OFI OCA].

	==See Also==		==See Also==
-	*[[Ubiquitin]]	+	*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]
		+	*[[Ubiquitin\|Ubiquitin]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~21185309~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:021185309</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
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	[[Category: Ralat, L A.]]		[[Category: Ralat, L A.]]
	[[Category: Tang, W J.]]		[[Category: Tang, W J.]]
		+	[[Category: Exosite]]
		+	[[Category: Human insulin-degrading enzyme]]
		+	[[Category: Hydrolase]]
		+	[[Category: Protein-peptide complex]]
		+	[[Category: Ubiquitin]]

OCA at 09:23, 23 February 2011

OCA — Wed, 23 Feb 2011 09:23:00 GMT

←Older revision		Revision as of 09:23, 23 February 2011
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	===Crystal structure of human insulin-degrading enzyme in complex with ubiquitin===		===Crystal structure of human insulin-degrading enzyme in complex with ubiquitin===

		+
		+	<!--
		+	The line below this paragraph, {{ABSTRACT_PUBMED_21185309}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 21185309 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_21185309}}

	==About this Structure==		==About this Structure==
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	==See Also==		==See Also==
	*[[Ubiquitin]]		*[[Ubiquitin]]
		+
		+	==Reference==
		+	<ref group="xtra">PMID:21185309</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
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	[[Category: Ralat, L A.]]		[[Category: Ralat, L A.]]
	[[Category: Tang, W J.]]		[[Category: Tang, W J.]]
-	[[Category: Exosite]]
-	[[Category: Human insulin-degrading enzyme]]
-	[[Category: Hydrolase]]
-	[[Category: Protein-peptide complex]]
-	[[Category: Ubiquitin]]

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

OCA — Sun, 26 Dec 2010 20:57:16 GMT

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

←Older revision

Revision as of 20:57, 26 December 2010

OCA at 20:57, 26 December 2010

OCA — Sun, 26 Dec 2010 20:57:15 GMT

←Older revision		Revision as of 20:57, 26 December 2010
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-	{{Seed}}
	[[Image:3ofi.png\|left\|200px]]		[[Image:3ofi.png\|left\|200px]]

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	==About this Structure==		==About this Structure==
-	~~3OFI~~ is a 4 ~~chains~~ structure with ~~sequences~~ 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=3OFI OCA].	+	[[3ofi]] is a 4 chain structure of [[Ubiquitin]] 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=3OFI OCA].
		+
		+	==See Also==
		+	*[[Ubiquitin]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
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	[[Category: Protein-peptide complex]]		[[Category: Protein-peptide complex]]
	[[Category: Ubiquitin]]		[[Category: Ubiquitin]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Sep 22 14:20:26 2010''