4lqg - Revision history

OCA at 11:19, 14 December 2022

OCA — Wed, 14 Dec 2022 11:19:22 GMT

←Older revision		Revision as of 11:19, 14 December 2022
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	==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056==		==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056==
-	<StructureSection load='4lqg' size='340' side='right' caption='[[4lqg]], [[Resolution\|resolution]] 1.77Å' scene=''>	+	<StructureSection load='4lqg' size='340' side='right'caption='[[4lqg]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4lqg]] 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=4LQG OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4LQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4lqg]] 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=4LQG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4LQG 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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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">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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [https://pdbe.org/4lqg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [https://www.ebi.ac.uk/pdbsum/4lqg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqg 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/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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [~~http~~://pdbe.org/4lqg PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4lqg PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqg 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 ==
Line 20:		Line 18:
	</div>		</div>
	<div class="pdbe-citations 4lqg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4lqg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carboxypeptidase 3D structures\|Carboxypeptidase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Glutamate carboxypeptidase II~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Barinka, C]]	+	[[Category: Barinka C]]
-	[[Category: Skultetyova, L]]	+	[[Category: Skultetyova L]]
-	~~[[Category: Hydrolase]]~~	+
-	~~[[Category: Hydrolase-hydrolase inhibitor complex]]~~	+
-	~~[[Category: Metallopeptidase]]~~	+
-	~~[[Category: Peptidase~~]]	+

OCA at 09:41, 15 November 2017

OCA — Wed, 15 Nov 2017 09:41:49 GMT

←Older revision		Revision as of 09:41, 15 November 2017
Line 3:		Line 3:
	<StructureSection load='4lqg' size='340' side='right' caption='[[4lqg]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='4lqg' size='340' side='right' caption='[[4lqg]], [[Resolution\|resolution]] 1.77Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4lqg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LQG FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4lqg]] 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=4LQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LQG 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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=~~NAG~~:N-~~ACETYL-D~~-~~GLUCOSAMINE~~'>~~NAG~~</scene>, <scene name='pdbligand=ZN:~~ZINC+ION~~'>ZN</scene>, <scene name='pdbligand=~~FUC~~:~~ALPHA~~-L-~~FUCOSE~~'>~~FUC~~</scene>, <scene name='pdbligand=~~MAN~~:~~ALPHA-D-MANNOSE~~'>~~MAN~~</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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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">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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [http://pdbe.org/4lqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [http://www.ebi.ac.uk/pdbsum/4lqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqg 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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [http://pdbe.org/4lqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [http://www.ebi.ac.uk/pdbsum/4lqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqg ProSAT]</span></td></tr>
Line 19:		Line 20:
	</div>		</div>
	<div class="pdbe-citations 4lqg" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4lqg" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Carboxypeptidase\|Carboxypeptidase]]
	== References ==		== References ==
	<references/>		<references/>
Line 27:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Glutamate carboxypeptidase II]]		[[Category: Glutamate carboxypeptidase II]]
		+	[[Category: Human]]
	[[Category: Barinka, C]]		[[Category: Barinka, C]]
	[[Category: Skultetyova, L]]		[[Category: Skultetyova, L]]

OCA at 17:33, 12 July 2016

OCA — Tue, 12 Jul 2016 17:33:08 GMT

←Older revision		Revision as of 17:33, 12 July 2016
Line 6:		Line 6:
	</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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [http://pdbe.org/4lqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [http://www.ebi.ac.uk/pdbsum/4lqg 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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [http://pdbe.org/4lqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [http://www.ebi.ac.uk/pdbsum/4lqg PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4lqg ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==

OCA at 07:34, 20 June 2016

OCA — Mon, 20 Jun 2016 07:34:00 GMT

←Older revision		Revision as of 07:34, 20 June 2016
Line 1:		Line 1:
		+
	==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056==		==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056==
	<StructureSection load='4lqg' size='340' side='right' caption='[[4lqg]], [[Resolution\|resolution]] 1.77Å' scene=''>		<StructureSection load='4lqg' size='340' side='right' caption='[[4lqg]], [[Resolution\|resolution]] 1.77Å' scene=''>
Line 5:		Line 6:
	</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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [http://www.ebi.ac.uk/pdbsum/4lqg 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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [http://pdbe.org/4lqg PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [http://www.ebi.ac.uk/pdbsum/4lqg PDBsum]</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.
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	A series of phosphoramidate-based prostate specific membrane antigen (PSMA) inhibitors of increasing lipophilicity were synthesized (4, 5, and 6), and their fluorine-18 analogs were evaluated for use as positron emission tomography (PET) imaging agents for prostate cancer. To gain insight into their modes of binding, they were also cocrystallized with the extracellular domain of PSMA. All analogs exhibited irreversible binding to PSMA with IC50 values ranging from 0.4 to 1.3 nM. In vitro assays showed binding and rapid internalization (80-95%, 2 h) of the radiolabeled ligands in PSMA(+) cells. In vivo distribution demonstrated significant uptake in CWR22Rv1 (PSMA(+)) tumor, with tumor to blood ratios of 25.6:1, 63.6:1, and 69.6:1 for [18F]4, [18F]5, and [18F]6, respectively, at 2 h postinjection. Installation of aminohexanoic acid (AH) linkers in the phosphoramidate scaffold improved their PSMA binding and inhibition and was critical for achieving suitable in vivo imaging properties, positioning [18F]5 and [18F]6 as favorable candidates for future prostate cancer imaging clinical trials.
		+
		+	Structure-Activity Relationship of F-Labeled Phosphoramidate Peptidomimetic Prostate-Specific Membrane Antigen (PSMA)-Targeted Inhibitor Analogues for PET Imaging of Prostate Cancer.,Dannoon S, Ganguly T, Cahaya H, Geruntho JJ, Galliher MS, Beyer SK, Choy CJ, Hopkins MR, Regan M, Blecha JE, Skultetyova L, Drake CR, Jivan S, Barinka C, Jones EF, Berkman CE, VanBrocklin HF J Med Chem. 2016 Jun 13. PMID:27228467<ref>PMID:27228467</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 4lqg" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carboxypeptidase\|Carboxypeptidase]]
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 14:49, 31 December 2014

OCA — Wed, 31 Dec 2014 14:49:52 GMT

←Older revision		Revision as of 14:49, 31 December 2014
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-	'''~~Unreleased structure~~'''	+	==X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056==
-		+	<StructureSection load='4lqg' size='340' side='right' caption='[[4lqg]], [[Resolution\|resolution]] 1.77Å' scene=''>
-	~~The entry~~ 4lqg is ~~ON HOLD until Paper Publication~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4lqg]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4LQG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4LQG FirstGlance]. <br>
-	~~Authors~~: ~~Barinka~~, C., ~~Skultetyova~~, L.	+	</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=CTW:N-(4-FLUOROBENZOYL)-L-GAMMA-GLUTAMYL-5-{[(S)-{[(1S)-1,3-DICARBOXYPROPYL]AMINO}(HYDROXY)PHOSPHORYL]OXY}-L-NORVALINE'>CTW</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene></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>
-	~~Description~~: X-~~ray structure of human~~ glutamate ~~carboxypeptidase II~~ (~~GCPII~~) in ~~complex with~~ a ~~phosphoramidate inhibitor CTT1056~~	+	<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=4lqg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lqg OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4lqg RCSB], [http://www.ebi.ac.uk/pdbsum/4lqg PDBsum]</span></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	</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__
		+	</StructureSection>
		+	[[Category: Glutamate carboxypeptidase II]]
	[[Category: Barinka, C]]		[[Category: Barinka, C]]
	[[Category: Skultetyova, L]]		[[Category: Skultetyova, L]]
		+	[[Category: Hydrolase]]
		+	[[Category: Hydrolase-hydrolase inhibitor complex]]
		+	[[Category: Metallopeptidase]]
		+	[[Category: Peptidase]]

OCA at 14:02, 24 December 2014

OCA — Wed, 24 Dec 2014 14:02:21 GMT

←Older revision		Revision as of 14:02, 24 December 2014
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	Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056		Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056
		+	[[Category: Unreleased Structures]]
		+	[[Category: Barinka, C]]
		+	[[Category: Skultetyova, L]]

OCA at 09:16, 25 December 2013

OCA — Wed, 25 Dec 2013 09:16:18 GMT

←Older revision		Revision as of 09:16, 25 December 2013
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	'''Unreleased structure'''		'''Unreleased structure'''

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

	Authors: Barinka, C., Skultetyova, L.		Authors: Barinka, C., Skultetyova, L.

	Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056		Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056

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

OCA — Wed, 24 Jul 2013 12:32:22 GMT

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

←Older revision

Revision as of 12:32, 24 July 2013

OCA: New page: '''Unreleased structure''' The entry 4lqg is ON HOLD Authors: Barinka, C., Skultetyova, L. Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a...

OCA — Wed, 24 Jul 2013 12:32:21 GMT

New page: '''Unreleased structure''' The entry 4lqg is ON HOLD Authors: Barinka, C., Skultetyova, L. Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a...

New page

'''Unreleased structure'''

The entry 4lqg is ON HOLD

Authors: Barinka, C., Skultetyova, L.

Description: X-ray structure of human glutamate carboxypeptidase II (GCPII) in complex with a phosphoramidate inhibitor CTT1056