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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='4ngm' size='340' side='right' caption='[[4ngm]], [[Resolution|resolution]] 1.84Å' scene=''> | <StructureSection load='4ngm' size='340' side='right' caption='[[4ngm]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ngn|4ngn]], [[4ngp|4ngp]], [[4ngq|4ngq]], [[4ngr|4ngr]], [[4ngs|4ngs]], [[4ngt|4ngt]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4ngn|4ngn]], [[4ngp|4ngp]], [[4ngq|4ngq]], [[4ngr|4ngr]], [[4ngs|4ngs]], [[4ngt|4ngt]]</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=4ngm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ngm RCSB], [http://www.ebi.ac.uk/pdbsum/4ngm 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=4ngm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ngm OCA], [http://pdbe.org/4ngm PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ngm RCSB], [http://www.ebi.ac.uk/pdbsum/4ngm PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ngm 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> | ||