4oc2: Difference between revisions

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 == Structural highlights ==
 <table><tr><td colspan='2'>[[4oc2]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OC2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OC2 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QQ:N~2~-{[(1S)-1-CARBOXYBUT-3-YN-1-YL]CARBAMOYL}-N~6~-(4-IODOBENZOYL)-L-LYSINE'>2QQ</scene>, <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=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><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=2QQ:N~2~-{[(1S)-1-CARBOXYBUT-3-YN-1-YL]CARBAMOYL}-N~6~-(4-IODOBENZOYL)-L-LYSINE'>2QQ</scene>, <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=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><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oc0|4oc0]], [[4oc1|4oc1]], [[4oc3|4oc3]], [[4oc4|4oc4]], [[4oc5|4oc5]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4oc0|4oc0]], [[4oc1|4oc1]], [[4oc3|4oc3]], [[4oc4|4oc4]], [[4oc5|4oc5]]</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=4oc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oc2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4oc2 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=4oc2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oc2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oc2 RCSB], [http://www.ebi.ac.uk/pdbsum/4oc2 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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 14: / Line 16: @@
 Structural characterization of P1'-diversified urea-based inhibitors of glutamate carboxypeptidase II.,Pavlicek J, Ptacek J, Cerny J, Byun Y, Skultetyova L, Pomper MG, Lubkowski J, Barinka C Bioorg Med Chem Lett. 2014 May 15;24(10):2340-5. doi: 10.1016/j.bmcl.2014.03.066., Epub 2014 Mar 28. PMID:24731280<ref>PMID:24731280</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
 == References ==
@@ Line 21: / Line 23: @@
 </StructureSection>
 [[Category: Glutamate carboxypeptidase II]]
-[[Category: Barinka, C.]]
+[[Category: Barinka, C]]
-[[Category: Byun, Y.]]
+[[Category: Byun, Y]]
-[[Category: Cerny, J.]]
+[[Category: Cerny, J]]
-[[Category: Lubkowski, J.]]
+[[Category: Lubkowski, J]]
-[[Category: Pavlicek, J.]]
+[[Category: Pavlicek, J]]
-[[Category: Pomper, M.]]
+[[Category: Pomper, M]]
-[[Category: Ptacek, J.]]
+[[Category: Ptacek, J]]
-[[Category: Skultetyova, L.]]
+[[Category: Skultetyova, L]]
 [[Category: Hydrolase]]
 [[Category: Hydrolase-hydrolase inhibitor complex]]
 [[Category: Metallopeptidase]]