4ome
From Proteopedia
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| - | ''' | + | ==X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety== |
| - | + | <StructureSection load='4ome' size='340' side='right' caption='[[4ome]], [[Resolution|resolution]] 1.79Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[4ome]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OME OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OME 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=DGQ:(S)-2-(3-((S)-1-CARBOXY-5-(1,2-DICARBA-CLOSO-DODECARBORANYLAMIDO)+PENTYL)UREIDO)PENTANEDIOIC+ACID'>DGQ</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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='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=4ome FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ome OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ome RCSB], [http://www.ebi.ac.uk/pdbsum/4ome PDBsum]</span></td></tr> | |
| - | [[Category: | + | </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: Ptacek, J]] | ||
[[Category: Byun, Y]] | [[Category: Byun, Y]] | ||
[[Category: Novakova, Z]] | [[Category: Novakova, Z]] | ||
| + | [[Category: Ptacek, J]] | ||
| + | [[Category: Hydrolase]] | ||
| + | [[Category: Hydrolase-hydrolase inhibitor complex]] | ||
| + | [[Category: Metallopeptidase]] | ||
Revision as of 13:06, 18 February 2015
X-ray structure of human glutamate carboxypeptidase II in complex with DCCBL, a urea based inhibitor with distal carborane moiety
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