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==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='4ngr' size='340' side='right' caption='[[4ngr]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='4ngr' size='340' side='right'caption='[[4ngr]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ngr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NGR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NGR FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ngr]] 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=4NGR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NGR 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=J21:N-{[(1S)-5-({2-[2-(ACETYLAMINO)ETHOXY]-4-BROMOBENZOYL}AMINO)-1-CARBOXYPENTYL]CARBAMOYL}-L-GLUTAMIC+ACID'>J21</scene>, <scene name='pdbligand= | </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=J21:N-{[(1S)-5-({2-[2-(ACETYLAMINO)ETHOXY]-4-BROMOBENZOYL}AMINO)-1-CARBOXYPENTYL]CARBAMOYL}-L-GLUTAMIC+ACID'>J21</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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3d7h|3d7h]], [[4ngm|4ngm]], [[4ngn|4ngn]], [[4ngp|4ngp]], [[4ngq|4ngq]], [[4ngs|4ngs]], [[4ngt|4ngt]]</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]], [[4ngs|4ngs]], [[4ngt|4ngt]]</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=4ngr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngr OCA], [http://pdbe.org/4ngr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ngr RCSB], [http://www.ebi.ac.uk/pdbsum/4ngr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngr 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=4ngr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngr OCA], [http://pdbe.org/4ngr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ngr RCSB], [http://www.ebi.ac.uk/pdbsum/4ngr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngr 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]] | ||
Revision as of 11:13, 10 April 2019
Crystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitorCrystal Structure of Glutamate Carboxypeptidase II in a complex with urea-based inhibitor
Structural highlights
Function[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 |
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