4yu9 - Revision history

OCA at 11:31, 9 May 2024

OCA — Thu, 09 May 2024 11:31:49 GMT

←Older revision		Revision as of 11:31, 9 May 2024
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4yu9]] is a 3 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=4YU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YU9 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4yu9]] is a 3 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=4YU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YU9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [https://pdbe.org/4yu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [https://www.ebi.ac.uk/pdbsum/4yu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu9 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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [https://pdbe.org/4yu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [https://www.ebi.ac.uk/pdbsum/4yu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu9 ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:26, 10 May 2023

OCA — Wed, 10 May 2023 07:26:04 GMT

←Older revision		Revision as of 07:26, 10 May 2023
Line 3:		Line 3:
	<StructureSection load='4yu9' size='340' side='right'caption='[[4yu9]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4yu9' size='340' side='right'caption='[[4yu9]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4yu9]] is a 3 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=4YU9 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4YU9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4yu9]] is a 3 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=4YU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YU9 FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">QPCT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [https://pdbe.org/4yu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [https://www.ebi.ac.uk/pdbsum/4yu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu9 ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [~~http~~://pdbe.org/4yu9 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4yu9 PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu9 ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>	+	[https://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Glutaminyl-peptide cyclotransferase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Benvenuti, M]]	+	[[Category: Benvenuti M]]
-	[[Category: ~~Mangani, S~~]]	+	[[Category: Di Pisa F]]
-	[[Category: ~~Pisa, F Di~~]]	+	[[Category: Mangani S]]
-	[[Category: Pozzi, C]]	+	[[Category: Pozzi C]]
-	~~[[Category: Alzheimer disease]]~~	+
-	~~[[Category: Drug target]]~~	+
-	~~[[Category: Transferase~~]]	+

OCA at 06:53, 12 June 2019

OCA — Wed, 12 Jun 2019 06:53:40 GMT

←Older revision		Revision as of 06:53, 12 June 2019
Line 1:		Line 1:

	==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase==		==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase==
-	<StructureSection load='4yu9' size='340' side='right' caption='[[4yu9]], [[Resolution\|resolution]] 2.10Å' scene=''>	+	<StructureSection load='4yu9' size='340' side='right'caption='[[4yu9]], [[Resolution\|resolution]] 2.10Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4yu9]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YU9 FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4yu9]] is a 3 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=4YU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YU9 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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">QPCT ([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/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [http://pdbe.org/4yu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu9 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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [http://pdbe.org/4yu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu9 ProSAT]</span></td></tr>
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4yu9" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4yu9" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Glutaminyl cyclase\|Glutaminyl cyclase]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 28:
	</StructureSection>		</StructureSection>
	[[Category: Glutaminyl-peptide cyclotransferase]]		[[Category: Glutaminyl-peptide cyclotransferase]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Benvenuti, M]]		[[Category: Benvenuti, M]]
	[[Category: Mangani, S]]		[[Category: Mangani, S]]

OCA at 14:15, 24 May 2017

OCA — Wed, 24 May 2017 14:15:36 GMT

←Older revision		Revision as of 14:15, 24 May 2017
Line 1:		Line 1:
		+
	==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase==		==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase==
	<StructureSection load='4yu9' size='340' side='right' caption='[[4yu9]], [[Resolution\|resolution]] 2.10Å' scene=''>		<StructureSection load='4yu9' size='340' side='right' caption='[[4yu9]], [[Resolution\|resolution]] 2.10Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yu9 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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [http://pdbe.org/4yu9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yu9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4yu9 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4yu9" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 06:29, 20 August 2015

OCA — Thu, 20 Aug 2015 06:29:45 GMT

←Older revision		Revision as of 06:29, 20 August 2015
Line 9:		Line 9:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>		[[http://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Recent developments in molecular pathology and genetics have allowed the identification of human glutaminyl cyclase (hQC) among the abnormal proteins involved in many neurodegenerative disorders. Difficulties in obtaining large quantities of pure protein may limit the use of crystallographic screening for drug development on this target. Site-directed mutagenesis experiments have led to the identification of some solvent-exposed residues that are absolutely critical to achieve increased solubility and to avoid precipitation of the enzyme in inclusion bodies when expressed in Escherichia coli. The designed variant Y115E-Y117E has been found to be able to provide large amounts of monodisperse, pure hQC from an E. coli expression system. To validate the use of the artificial construct as a target for large-scale X-ray and NMR screening campaigns in the search for new inhibitors of hQC, the X-ray crystal structures of the hQC Y115E-Y117E variant and of its adduct with the inhibitor PBD-150 were determined.
		+
		+	The soluble Y115E-Y117E variant of human glutaminyl cyclase is a valid target for X-ray and NMR screening of inhibitors against Alzheimer disease.,DiPisa F, Pozzi C, Benvenuti M, Andreini M, Marconi G, Mangani S Acta Crystallogr F Struct Biol Commun. 2015 Aug 1;71(Pt 8):986-92. doi:, 10.1107/S2053230X15010389. Epub 2015 Jul 28. PMID:26249687<ref>PMID:26249687</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:15, 5 August 2015

OCA — Wed, 05 Aug 2015 20:15:11 GMT

←Older revision		Revision as of 20:15, 5 August 2015
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase==
-		+	<StructureSection load='4yu9' size='340' side='right' caption='[[4yu9]], [[Resolution\|resolution]] 2.10Å' scene=''>
-	~~The entry~~ 4yu9 is ~~ON HOLD~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4yu9]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4YU9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YU9 FirstGlance]. <br>
-	~~Authors~~: ~~Di Pisa~~, F., ~~Pozzi~~, C., ~~Benvenuti~~, M., ~~Mangani~~, S.	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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/Glutaminyl-peptide_cyclotransferase Glutaminyl-peptide cyclotransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.5 2.3.2.5] </span></td></tr>
-	~~Description~~: ~~Crystal Structure~~ of ~~double mutant Y115E Y117E human Glutaminyl Cyclase~~	+	<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=4yu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4yu9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4yu9 RCSB], [http://www.ebi.ac.uk/pdbsum/4yu9 PDBsum]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/QPCT_HUMAN QPCT_HUMAN]] Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-beta-amyloid. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.<ref>PMID:15063747</ref> <ref>PMID:18486145</ref> <ref>PMID:21288892</ref>
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Glutaminyl-peptide cyclotransferase]]
	[[Category: Benvenuti, M]]		[[Category: Benvenuti, M]]
-	[[Category: Pozzi, C]]
	[[Category: Mangani, S]]		[[Category: Mangani, S]]
-	[[Category: Di Pisa, F]]	+	[[Category: Pisa, F Di]]
		+	[[Category: Pozzi, C]]
		+	[[Category: Alzheimer disease]]
		+	[[Category: Drug target]]
		+	[[Category: Transferase]]

OCA: Protected "4yu9" [edit=sysop:move=sysop]

OCA — Thu, 26 Mar 2015 12:51:18 GMT

Protected "4yu9" [edit=sysop:move=sysop]

←Older revision

Revision as of 12:51, 26 March 2015

OCA: New page: '''Unreleased structure''' The entry 4yu9 is ON HOLD Authors: Di Pisa, F., Pozzi, C., Benvenuti, M., Mangani, S. Description: Crystal Structure of double mutant Y115E Y117E human Gluta...

OCA — Thu, 26 Mar 2015 12:51:17 GMT

New page: '''Unreleased structure''' The entry 4yu9 is ON HOLD Authors: Di Pisa, F., Pozzi, C., Benvenuti, M., Mangani, S. Description: Crystal Structure of double mutant Y115E Y117E human Gluta...

New page

'''Unreleased structure'''

The entry 4yu9 is ON HOLD

Authors: Di Pisa, F., Pozzi, C., Benvenuti, M., Mangani, S.

Description: Crystal Structure of double mutant Y115E Y117E human Glutaminyl Cyclase
[[Category: Unreleased Structures]]
[[Category: Benvenuti, M]]
[[Category: Pozzi, C]]
[[Category: Mangani, S]]
[[Category: Di Pisa, F]]