4ngt - Revision history

OCA at 08:28, 11 January 2023

2023-01-11T08:28:06Z

←Older revision		Revision as of 08:28, 11 January 2023
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	<StructureSection load='4ngt' size='340' side='right'caption='[[4ngt]], [[Resolution\|resolution]] 2.31Å' scene=''>		<StructureSection load='4ngt' size='340' side='right'caption='[[4ngt]], [[Resolution\|resolution]] 2.31Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ngt]] is a 1 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=4NGT OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4NGT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ngt]] is a 1 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=4NGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NGT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J42:N-{[(1S)-5-({[4-bromo-2-({4,44-dioxo-48-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-7,10,13,16,19,22,25,28,31,34,37,40-dodecaoxa-3,43-diazaoctatetracont-1-yl}oxy)phenyl]carbamoyl}amino)-1-carboxypentyl]carbamoyl}-L-glutamic+acid'>J42</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J42:N-{[(1S)-5-({[4-bromo-2-({4,44-dioxo-48-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-7,10,13,16,19,22,25,28,31,34,37,40-dodecaoxa-3,43-diazaoctatetracont-1-yl}oxy)phenyl]carbamoyl}amino)-1-carboxypentyl]carbamoyl}-L-glutamic+acid'>J42</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <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">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</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=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [https://pdbe.org/4ngt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [https://www.ebi.ac.uk/pdbsum/4ngt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngt ProSAT]</span></td></tr>
-	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA ([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/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </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=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [~~http~~://pdbe.org/4ngt PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4ngt PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngt ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.	+	[https://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
	<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: ~~Glutamate carboxypeptidase II]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Pachl, P]]	+	[[Category: Pachl P]]
-	[[Category: Tykvart, J]]	+	[[Category: Tykvart J]]
-	~~[[Category: Caboxypeptidase]]~~	+
-	~~[[Category: Glutamate carboxypeptidase ii]]~~	+
-	~~[[Category: Glycoprotein]]~~	+
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Metallopeptidase]]~~	+
-	~~[[Category: Naaladase]]~~	+
-	~~[[Category: Psma]]~~	+
-	~~[[Category: Urea-based inhibitor~~]]	+

OCA at 08:21, 18 December 2019

2019-12-18T08:21:01Z

←Older revision		Revision as of 08:21, 18 December 2019
Line 12:		Line 12:
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.		[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Glutamate carboxypeptidase II (GCPII), also known as prostate specific membrane antigen (PSMA), is an established prostate cancer marker and is considered a promising target for specific anticancer drug delivery. Low-molecular-weight inhibitors of GCPII are advantageous specific ligands for this purpose. However, they must be modified with a linker to enable connection of the ligand with an imaging molecule, anticancer drug, and/or nanocarrier. Here, we describe a structure-activity relationship (SAR) study of GCPII inhibitors with linkers suitable for imaging and drug delivery. Structure-assisted inhibitor design and targeting of a specific GCPII exosite resulted in a 7-fold improvement in Ki value compared to the parent structure. X-ray structural analysis of the inhibitor series led to the identification of several inhibitor binding modes. We also optimized the length of the inhibitor linker for effective attachment to a biotin-binding molecule and showed that the optimized inhibitor could be used to target nanoparticles to cells expressing GCPII.
		+
		+	Rational design of urea-based glutamate carboxypeptidase II (GCPII) inhibitors as versatile tools for specific drug targeting and delivery.,Tykvart J, Schimer J, Barinkova J, Pachl P, Postova-Slavetinska L, Majer P, Konvalinka J, Sacha P Bioorg Med Chem. 2014 Aug 1;22(15):4099-108. doi: 10.1016/j.bmc.2014.05.061. Epub, 2014 Jun 5. PMID:24954515<ref>PMID:24954515</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4ngt" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
-	*[[Carboxypeptidase\|Carboxypeptidase]]	+	*[[Carboxypeptidase 3D structures\|Carboxypeptidase 3D structures]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 08:19, 10 April 2019

2019-04-10T08:19:42Z

←Older revision		Revision as of 08:19, 10 April 2019
Line 1:		Line 1:

	==Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor==		==Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor==
-	<StructureSection load='4ngt' size='340' side='right' caption='[[4ngt]], [[Resolution\|resolution]] 2.31Å' scene=''>	+	<StructureSection load='4ngt' size='340' side='right'caption='[[4ngt]], [[Resolution\|resolution]] 2.31Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4ngt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NGT FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4ngt]] is a 1 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=4NGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NGT FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J42:N-{[(1S)-5-({[4-~~BROMO~~-2-({4,44-~~DIOXO~~-48-[(~~3AS~~,4S,~~6AR~~)-2-~~OXOHEXAHYDRO~~-1H-~~THIENO~~[3,4-D]~~IMIDAZOL~~-4-YL]-7,10,13,16,19,22,25,28,31,34,37,40-~~DODECAOXA~~-3,43-~~DIAZAOCTATETRACONT~~-1-YL}~~OXY~~)~~PHENYL~~]~~CARBAMOYL~~}~~AMINO~~)-1-~~CARBOXYPENTYL~~]~~CARBAMOYL~~}-L-~~GLUTAMIC~~+~~ACID~~'>J42</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J42:N-{[(1S)-5-({[4-bromo-2-({4,44-dioxo-48-[(3aS,4S,6aR)-2-oxohexahydro-1H-thieno[3,4-d]imidazol-4-yl]-7,10,13,16,19,22,25,28,31,34,37,40-dodecaoxa-3,43-diazaoctatetracont-1-yl}oxy)phenyl]carbamoyl}amino)-1-carboxypentyl]carbamoyl}-L-glutamic+acid'>J42</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <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">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">FOLH, FOLH1, GIG27, NAALAD1, PSM, PSMA ([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/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </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=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [http://pdbe.org/4ngt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [http://www.ebi.ac.uk/pdbsum/4ngt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngt 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=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [http://pdbe.org/4ngt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [http://www.ebi.ac.uk/pdbsum/4ngt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngt ProSAT]</span></td></tr>
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	</StructureSection>		</StructureSection>
	[[Category: Glutamate carboxypeptidase II]]		[[Category: Glutamate carboxypeptidase II]]
		+	[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Pachl, P]]		[[Category: Pachl, P]]
	[[Category: Tykvart, J]]		[[Category: Tykvart, J]]

OCA at 11:06, 4 August 2016

2016-08-04T11:06:29Z

←Older revision		Revision as of 11:06, 4 August 2016
Line 1:		Line 1:
		+
	==Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor==		==Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor==
	<StructureSection load='4ngt' size='340' side='right' caption='[[4ngt]], [[Resolution\|resolution]] 2.31Å' scene=''>		<StructureSection load='4ngt' size='340' side='right' caption='[[4ngt]], [[Resolution\|resolution]] 2.31Å' scene=''>
Line 6:		Line 7:
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </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=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [http://www.ebi.ac.uk/pdbsum/4ngt 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=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [http://pdbe.org/4ngt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [http://www.ebi.ac.uk/pdbsum/4ngt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngt ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.		[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
		+
		+	==See Also==
		+	*[[Carboxypeptidase\|Carboxypeptidase]]
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 13:39, 24 December 2014

2014-12-24T13:39:14Z

←Older revision		Revision as of 13:39, 24 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4ngt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NGT FirstGlance]. <br>		<table><tr><td colspan='2'>[[4ngt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NGT FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J42:N-{[(1S)-5-({[4-BROMO-2-({4,44-DIOXO-48-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]-7,10,13,16,19,22,25,28,31,34,37,40-DODECAOXA-3,43-DIAZAOCTATETRACONT-1-YL}OXY)PHENYL]CARBAMOYL}AMINO)-1-CARBOXYPENTYL]CARBAMOYL}-L-GLUTAMIC+ACID'>J42</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J42:N-{[(1S)-5-({[4-BROMO-2-({4,44-DIOXO-48-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]-7,10,13,16,19,22,25,28,31,34,37,40-DODECAOXA-3,43-DIAZAOCTATETRACONT-1-YL}OXY)PHENYL]CARBAMOYL}AMINO)-1-CARBOXYPENTYL]CARBAMOYL}-L-GLUTAMIC+ACID'>J42</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</td></tr>
-	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [http://www.ebi.ac.uk/pdbsum/4ngt 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=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [http://www.ebi.ac.uk/pdbsum/4ngt PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/FOLH1_HUMAN FOLH1_HUMAN]] Has both folate hydrolase and N-acetylated-alpha-linked-acidic dipeptidase (NAALADase) activity. Has a preference for tri-alpha-glutamate peptides. In the intestine, required for the uptake of folate. In the brain, modulates excitatory neurotransmission through the hydrolysis of the neuropeptide, N-aceylaspartylglutamate (NAAG), thereby releasing glutamate. Isoform PSM-4 and isoform PSM-5 would appear to be physiologically irrelevant. Involved in prostate tumor progression. Also exhibits a dipeptidyl-peptidase IV type activity. In vitro, cleaves Gly-Pro-AMC.
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: Glutamate carboxypeptidase II]]		[[Category: Glutamate carboxypeptidase II]]
-	[[Category: Pachl, P.]]	+	[[Category: Pachl, P]]
-	[[Category: Tykvart, J.]]	+	[[Category: Tykvart, J]]
	[[Category: Caboxypeptidase]]		[[Category: Caboxypeptidase]]
	[[Category: Glutamate carboxypeptidase ii]]		[[Category: Glutamate carboxypeptidase ii]]

OCA at 08:15, 18 June 2014

2014-06-18T08:15:42Z

←Older revision		Revision as of 08:15, 18 June 2014
Line 1:		Line 1:
-	'''~~Unreleased structure~~'''	+	==Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor==
-		+	<StructureSection load='4ngt' size='340' side='right' caption='[[4ngt]], [[Resolution\|resolution]] 2.31Å' scene=''>
-	~~The entry~~ 4ngt is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4ngt]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NGT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NGT FirstGlance]. <br>
-	~~Authors~~: ~~Tykvart~~, J., Pachl, P.	+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=J42:N-{[(1S)-5-({[4-BROMO-2-({4,44-DIOXO-48-[(3AS,4S,6AR)-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]-7,10,13,16,19,22,25,28,31,34,37,40-DODECAOXA-3,43-DIAZAOCTATETRACONT-1-YL}OXY)PHENYL]CARBAMOYL}AMINO)-1-CARBOXYPENTYL]CARBAMOYL}-L-GLUTAMIC+ACID'>J42</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
-		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3d7h\|3d7h]], [[4ngm\|4ngm]], [[4ngn\|4ngn]], [[4ngp\|4ngp]], [[4ngq\|4ngq]], [[4ngr\|4ngr]], [[4ngs\|4ngs]]</td></tr>
-	~~Description~~: ~~Crystal Structure of~~ Glutamate ~~Carboxypeptidase II in a~~ complex ~~with urea~~-based inhibitor	+	<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutamate_carboxypeptidase_II Glutamate carboxypeptidase II], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.17.21 3.4.17.21] </span></td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ngt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngt OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ngt RCSB], [http://www.ebi.ac.uk/pdbsum/4ngt PDBsum]</span></td></tr>
		+	<table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Glutamate carboxypeptidase II]]
		+	[[Category: Pachl, P.]]
		+	[[Category: Tykvart, J.]]
		+	[[Category: Caboxypeptidase]]
		+	[[Category: Glutamate carboxypeptidase ii]]
		+	[[Category: Glycoprotein]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Metallopeptidase]]
		+	[[Category: Naaladase]]
		+	[[Category: Psma]]
		+	[[Category: Urea-based inhibitor]]

OCA at 09:23, 25 December 2013

2013-12-25T09:23:42Z

←Older revision		Revision as of 09:23, 25 December 2013
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Tykvart, J., Pachl, P.		Authors: Tykvart, J., Pachl, P.

	Description: Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor		Description: Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor

OCA at 09:16, 18 December 2013

2013-12-18T09:16:00Z

←Older revision		Revision as of 09:16, 18 December 2013
Line 3:		Line 3:
	The entry 4ngt is ON HOLD		The entry 4ngt is ON HOLD

-	Authors: Tykvart, J., Pachl P.	+	Authors: Tykvart, J., Pachl, P.

	Description: Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor		Description: Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor

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

2013-11-13T07:48:22Z

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

←Older revision

Revision as of 07:48, 13 November 2013

OCA: New page: '''Unreleased structure''' The entry 4ngt is ON HOLD Authors: Tykvart, J., Pachl P. Description: Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibit...

2013-11-13T07:48:21Z

New page: '''Unreleased structure''' The entry 4ngt is ON HOLD Authors: Tykvart, J., Pachl P. Description: Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibit...

New page

'''Unreleased structure'''

The entry 4ngt is ON HOLD

Authors: Tykvart, J., Pachl P.

Description: Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor