3e4z - Revision history

OCA at 09:44, 21 February 2024

2024-02-21T09:44:40Z

←Older revision		Revision as of 09:44, 21 February 2024
Line 3:		Line 3:
	<StructureSection load='3e4z' size='340' side='right'caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='3e4z' size='340' side='right'caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e4z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e4z]] 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=3E4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4Z FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<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]] 2.28Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>~~[[~~Related_structure~~\|~~Related:~~]]~~</b></td><td class="sblockDat"><div style='overflow: auto~~; ~~max-height: 3em;'>[[3e50\|3e50]]</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&~~id=~~9606 HUMAN]), IGF2 ([https://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~~'>~~[https://en.wikipedia.org/wiki/Insulysin Insulysin], with EC number [https://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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [https://pdbe.org/3e4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [https://www.ebi.ac.uk/pdbsum/3e4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4z 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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [https://pdbe.org/3e4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [https://www.ebi.ac.uk/pdbsum/3e4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4z ProSAT]</span></td></tr>
	</table>		</table>
-	== Disease ==
-	[[https://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause of Silver-Russell syndrome (SRS) [MIM:[https://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.<ref>PMID:19066168</ref>
	== Function ==		== Function ==
-	[[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> [[https://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.<ref>PMID:16912056</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]]
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	</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=3e4z 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=3e4z ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
-	<div style="background-color:#fffaf0;">
-	== Publication Abstract from PubMed ==
-	Insulin-degrading enzyme (IDE) is involved in the clearance of many bioactive peptide substrates, including insulin and amyloid-beta, peptides vital to the development of diabetes and Alzheimer's disease, respectively. IDE can also rapidly degrade hormones that are held together by intramolecular disulfide bond(s) without their reduction. Furthermore, IDE exhibits a remarkable ability to preferentially degrade structurally similar peptides such as the selective degradation of insulin-like growth factor (IGF)-II and transforming growth factor-alpha (TGF-alpha) over IGF-I and epidermal growth factor, respectively. Here, we used high-accuracy mass spectrometry to identify the cleavage sites of human IGF-II, TGF-alpha, amylin, reduced amylin, and amyloid-beta by human IDE. We also determined the structures of human IDE-IGF-II and IDE-TGF-alpha at 2.3 A and IDE-amylin at 2.9 A. We found that IDE cleaves its substrates at multiple sites in a biased stochastic manner. Furthermore, the presence of a disulfide bond in amylin allows IDE to cut at an additional site in the middle of the peptide (amino acids 18-19). Our amylin-bound IDE structure offers insight into how the structural constraint from a disulfide bond in amylin can alter IDE cleavage sites. Together with NMR structures of amylin and the IGF and epidermal growth factor families, our work also reveals the structural basis of how the high dipole moment of substrates complements the charge distribution of the IDE catalytic chamber for the substrate selectivity. In addition, we show how the ability of substrates to properly anchor their N-terminus to the exosite of IDE and undergo a conformational switch upon binding to the catalytic chamber of IDE can also contribute to the selective degradation of structurally related growth factors.
-
-	Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme.,Guo Q, Manolopoulou M, Bian Y, Schilling AB, Tang WJ J Mol Biol. 2010 Jan 15;395(2):430-43. Epub 2009 Nov 5. PMID:19896952<ref>PMID:19896952</ref>
-
-	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	</div>
-	<div class="pdbe-citations 3e4z" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Insulysin~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Guo, Q]]	+	[[Category: Guo Q]]
-	[[Category: Manolopoulou, M]]	+	[[Category: Manolopoulou M]]
-	[[Category: Tang, W J]]	+	[[Category: Tang W-J]]
-	~~[[Category: Alternative splicing]]~~	+
-	~~[[Category: Complex]]~~	+
-	~~[[Category: Degrading]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Growth factor]]~~	+
-	~~[[Category: Hydrolase-hormone complex]]~~	+
-	~~[[Category: Ide]]~~	+
-	~~[[Category: Igf-ii]]~~	+
-	~~[[Category: Mitogen]]~~	+
-	~~[[Category: Polymorphism]]~~	+
-	~~[[Category: Secreted~~]]	+

OCA at 19:35, 20 October 2021

2021-10-20T19:35:32Z

←Older revision		Revision as of 19:35, 20 October 2021
Line 1:		Line 1:

	==Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II==		==Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II==
-	<StructureSection load='3e4z' size='340' side='right' caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>	+	<StructureSection load='3e4z' size='340' side='right'caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e4z]] 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=3E4Z OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3E4Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e4z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3E4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3E4Z FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e50\|3e50]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3e50\|3e50]]</div></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]), IGF2 ([~~http~~://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>	+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">IDE ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), IGF2 ([https://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'>[https://en.wikipedia.org/wiki/Insulysin Insulysin], with EC number [https://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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [~~http~~://pdbe.org/3e4z PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3e4z PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4z 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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [https://pdbe.org/3e4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [https://www.ebi.ac.uk/pdbsum/3e4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4z ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause of Silver-Russell syndrome (SRS) [MIM:[~~http~~://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.<ref>PMID:19066168</ref>	+	[[https://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause of Silver-Russell syndrome (SRS) [MIM:[https://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.<ref>PMID:19066168</ref>
	== 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/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.<ref>PMID:16912056</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> [[https://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.<ref>PMID:16912056</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
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	==See Also==		==See Also==
-	*[[Insulin-~~Degrading Enzyme~~\|Insulin-~~Degrading Enzyme~~]]	+	*[[Insulin-degrading enzyme 3D structures\|Insulin-degrading enzyme 3D structures]]
	*[[Insulin-like growth factor\|Insulin-like growth factor]]		*[[Insulin-like growth factor\|Insulin-like growth factor]]
	== References ==		== References ==
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	[[Category: Human]]		[[Category: Human]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
		+	[[Category: Large Structures]]
	[[Category: Guo, Q]]		[[Category: Guo, Q]]
	[[Category: Manolopoulou, M]]		[[Category: Manolopoulou, M]]

OCA at 21:42, 2 December 2018

2018-12-02T21:42:13Z

←Older revision		Revision as of 21:42, 2 December 2018
Line 1:		Line 1:
		+
	==Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II==		==Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II==
	<StructureSection load='3e4z' size='340' side='right' caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='3e4z' size='340' side='right' caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>
Line 7:		Line 8:
	<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]), IGF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]), IGF2 ([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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [http://pdbe.org/3e4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [http://www.ebi.ac.uk/pdbsum/3e4z 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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [http://pdbe.org/3e4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [http://www.ebi.ac.uk/pdbsum/3e4z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3e4z ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 17:		Line 18:
	Check<jmol>		Check<jmol>
	<jmolCheckbox>		<jmolCheckbox>
-	<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/3e4z_consurf.spt"</scriptWhenChecked>	+	<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/e4/3e4z_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 45:		Line 46:
	[[Category: Manolopoulou, M]]		[[Category: Manolopoulou, M]]
	[[Category: Tang, W J]]		[[Category: Tang, W J]]
		+	[[Category: Alternative splicing]]
	[[Category: Complex]]		[[Category: Complex]]
	[[Category: Degrading]]		[[Category: Degrading]]
Line 53:		Line 55:
	[[Category: Igf-ii]]		[[Category: Igf-ii]]
	[[Category: Mitogen]]		[[Category: Mitogen]]
		+	[[Category: Polymorphism]]
	[[Category: Secreted]]		[[Category: Secreted]]

OCA at 14:57, 9 February 2016

2016-02-09T14:57:08Z

←Older revision		Revision as of 14:57, 9 February 2016
Line 2:		Line 2:
	<StructureSection load='3e4z' size='340' side='right' caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>		<StructureSection load='3e4z' size='340' side='right' caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3e4z]] 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=3E4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E4Z FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3e4z]] 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=3E4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E4Z FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e50\|3e50]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e50\|3e50]]</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~~]), IGF2 ([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]), IGF2 ([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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [http://www.ebi.ac.uk/pdbsum/3e4z 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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [http://pdbe.org/3e4z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [http://www.ebi.ac.uk/pdbsum/3e4z PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
	[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause of Silver-Russell syndrome (SRS) [MIM:[http://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.<ref>PMID:19066168</ref>		[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause of Silver-Russell syndrome (SRS) [MIM:[http://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.<ref>PMID:19066168</ref>
	== Function ==		== Function ==
-	[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.<ref>PMID:16912056</ref>	+	[[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/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.<ref>PMID:16912056</ref>
	== Evolutionary Conservation ==		== Evolutionary Conservation ==
	[[Image:Consurf_key_small.gif\|200px\|right]]		[[Image:Consurf_key_small.gif\|200px\|right]]
Line 21:		Line 21:
	<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=3e4z ConSurf].
	<div style="clear:both"></div>		<div style="clear:both"></div>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
Line 31:		Line 31:
	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 3e4z" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 39:		Line 40:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
	[[Category: Guo, Q]]		[[Category: Guo, Q]]

OCA at 13:41, 18 December 2014

2014-12-18T13:41:31Z

←Older revision		Revision as of 13:41, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_3e4z\| PDB=3e4z \| SCENE= }}~~	+	==Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II==
-	===Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II===	+	<StructureSection load='3e4z' size='340' side='right' caption='[[3e4z]], [[Resolution\|resolution]] 2.28Å' scene=''>
-	~~{{ABSTRACT_PUBMED_19896952}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3e4z]] 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=3E4Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3E4Z FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3e50\|3e50]]</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]), IGF2 ([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=3e4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3e4z OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3e4z RCSB], [http://www.ebi.ac.uk/pdbsum/3e4z PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause of Silver-Russell syndrome (SRS) [MIM:[http://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.<ref>PMID:19066168</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.<ref>PMID:16912056</ref>
		+	== 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/e4/3e4z_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) is involved in the clearance of many bioactive peptide substrates, including insulin and amyloid-beta, peptides vital to the development of diabetes and Alzheimer's disease, respectively. IDE can also rapidly degrade hormones that are held together by intramolecular disulfide bond(s) without their reduction. Furthermore, IDE exhibits a remarkable ability to preferentially degrade structurally similar peptides such as the selective degradation of insulin-like growth factor (IGF)-II and transforming growth factor-alpha (TGF-alpha) over IGF-I and epidermal growth factor, respectively. Here, we used high-accuracy mass spectrometry to identify the cleavage sites of human IGF-II, TGF-alpha, amylin, reduced amylin, and amyloid-beta by human IDE. We also determined the structures of human IDE-IGF-II and IDE-TGF-alpha at 2.3 A and IDE-amylin at 2.9 A. We found that IDE cleaves its substrates at multiple sites in a biased stochastic manner. Furthermore, the presence of a disulfide bond in amylin allows IDE to cut at an additional site in the middle of the peptide (amino acids 18-19). Our amylin-bound IDE structure offers insight into how the structural constraint from a disulfide bond in amylin can alter IDE cleavage sites. Together with NMR structures of amylin and the IGF and epidermal growth factor families, our work also reveals the structural basis of how the high dipole moment of substrates complements the charge distribution of the IDE catalytic chamber for the substrate selectivity. In addition, we show how the ability of substrates to properly anchor their N-terminus to the exosite of IDE and undergo a conformational switch upon binding to the catalytic chamber of IDE can also contribute to the selective degradation of structurally related growth factors.

-	~~==Disease==~~	+	Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme.,Guo Q, Manolopoulou M, Bian Y, Schilling AB, Tang WJ J Mol Biol. 2010 Jan 15;395(2):430-43. Epub 2009 Nov 5. PMID:19896952<ref>PMID:19896952</ref>
-	~~[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause~~ of ~~Silver~~-~~Russell syndrome (SRS) [MIM:[http://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation~~, ~~poor postnatal growth~~, ~~craniofacial features such as a triangular shaped face~~ and ~~a broad forehead~~, ~~body asymmetry~~, ~~and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence~~, ~~with the facial features and asymmetry usually becoming more subtle with age~~.<ref>PMID:~~19066168~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro~~, ~~they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play~~ a ~~role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier~~ of ~~glucose-mediated insulin secretion~~. ~~Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation~~ of ~~MAPK1 and MAPK3~~.<~~ref~~>~~PMID:16912056~~</~~ref~~>	+	</div>
-		+
-	~~==About this Structure==~~	+
-	[[3e4z]] 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=3E4Z OCA].	+

	==See Also==		==See Also==
	*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]		*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]
	*[[Insulin-like growth factor\|Insulin-like growth factor]]		*[[Insulin-like growth factor\|Insulin-like growth factor]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:019896952</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
-	[[Category: Guo, Q.]]	+	[[Category: Guo, Q]]
-	[[Category: Manolopoulou, M.]]	+	[[Category: Manolopoulou, M]]
-	[[Category: Tang, W J.]]	+	[[Category: Tang, W J]]
	[[Category: Complex]]		[[Category: Complex]]
	[[Category: Degrading]]		[[Category: Degrading]]

OCA at 11:05, 24 March 2013

2013-03-24T11:05:24Z

←Older revision		Revision as of 11:05, 24 March 2013
Line 1:		Line 1:
-	[[Image:3e4z.png\|left\|200px]]
-
	{{STRUCTURE_3e4z\| PDB=3e4z \| SCENE= }}		{{STRUCTURE_3e4z\| PDB=3e4z \| SCENE= }}
-
	===Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II===		===Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II===
		+	{{ABSTRACT_PUBMED_19896952}}

-	~~{{ABSTRACT_PUBMED_19896952}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] Epigenetic changes of DNA hypomethylation in IGF2 are a cause of Silver-Russell syndrome (SRS) [MIM:[http://omim.org/entry/180860 180860]]. A clinically heterogeneous condition characterized by severe intrauterine growth retardation, poor postnatal growth, craniofacial features such as a triangular shaped face and a broad forehead, body asymmetry, and a variety of minor malformations. The phenotypic expression changes during childhood and adolescence, with the facial features and asymmetry usually becoming more subtle with age.<ref>PMID:19066168</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/IGF2_HUMAN IGF2_HUMAN]] The insulin-like growth factors possess growth-promoting activity. In vitro, they are potent mitogens for cultured cells. IGF-II is influenced by placental lactogen and may play a role in fetal development.<ref>PMID:16912056</ref> Preptin undergoes glucose-mediated co-secretion with insulin, and acts as physiological amplifier of glucose-mediated insulin secretion. Exhibits osteogenic properties by increasing osteoblast mitogenic activity through phosphoactivation of MAPK1 and MAPK3.<ref>PMID:16912056</ref>

	==About this Structure==		==About this Structure==
Line 15:		Line 17:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:019896952</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019896952</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Insulysin]]		[[Category: Insulysin]]

OCA at 14:13, 20 October 2012

2012-10-20T14:13:35Z

←Older revision		Revision as of 14:13, 20 October 2012
Line 8:		Line 8:

	==About this Structure==		==About this Structure==
-	[[3e4z]] is a 4 chain structure ~~of [[Insulin-Degrading Enzyme]]~~ 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=3E4Z OCA].	+	[[3e4z]] 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=3E4Z OCA].

	==See Also==		==See Also==
	*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]		*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]
		+	*[[Insulin-like growth factor\|Insulin-like growth factor]]

	==Reference==		==Reference==

OCA: Protected "3e4z" [edit=sysop:move=sysop]

2012-07-26T14:28:41Z

Protected "3e4z" [edit=sysop:move=sysop]

←Older revision

Revision as of 14:28, 26 July 2012

OCA at 14:28, 26 July 2012

2012-07-26T14:28:39Z

←Older revision		Revision as of 14:28, 26 July 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:3e4z.png\|left\|200px]]		[[Image:3e4z.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_3e4z", 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),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_3e4z\| PDB=3e4z \| SCENE= }}		{{STRUCTURE_3e4z\| PDB=3e4z \| SCENE= }}

	===Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II===		===Crystal structure of human insulin degrading enzyme in complex with insulin-like growth factor II===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_19896952}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 19896952 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_19896952}}		{{ABSTRACT_PUBMED_19896952}}
-
-	==Disease==
-	Known disease associated with this structure: Intrauterine and postnatal growth retardation OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147470 147470]]

	==About this Structure==		==About this Structure==
-	~~3E4Z~~ 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=3E4Z OCA].	+	[[3e4z]] is a 4 chain structure of [[Insulin-Degrading Enzyme]] 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=3E4Z OCA].
		+
		+	==See Also==
		+	*[[Insulin-Degrading Enzyme\|Insulin-Degrading Enzyme]]

	==Reference==		==Reference==
-	<ref group="xtra">PMID:~~19896952~~</ref><references group="xtra"/>	+	<ref group="xtra">PMID:019896952</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Insulysin]]		[[Category: Insulysin]]
Line 32:		Line 20:
	[[Category: Manolopoulou, M.]]		[[Category: Manolopoulou, M.]]
	[[Category: Tang, W J.]]		[[Category: Tang, W J.]]
-	[[Category: Alternative splicing]]
	[[Category: Complex]]		[[Category: Complex]]
	[[Category: Degrading]]		[[Category: Degrading]]
	[[Category: Glycoprotein]]		[[Category: Glycoprotein]]
	[[Category: Growth factor]]		[[Category: Growth factor]]
-	[[Category: Hydrolase/hormone complex]]	+	[[Category: Hydrolase-hormone complex]]
	[[Category: Ide]]		[[Category: Ide]]
	[[Category: Igf-ii]]		[[Category: Igf-ii]]
	[[Category: Mitogen]]		[[Category: Mitogen]]
-	[[Category: Polymorphism]]
	[[Category: Secreted]]		[[Category: Secreted]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 15:53:16 2010''

OCA at 13:53, 10 February 2010

2010-02-10T13:53:17Z

←Older revision		Revision as of 13:53, 10 February 2010
Line 23:		Line 23:

	==About this Structure==		==About this Structure==
-	3E4Z is a 4 chains structure of 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=3E4Z OCA].	+	3E4Z 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=3E4Z OCA].

	==Reference==		==Reference==
Line 44:		Line 44:
	[[Category: Secreted]]		[[Category: Secreted]]

-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed ~~Dec 9 14~~:02:~~12 2009~~''	+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 15:53:16 2010''