2jbj

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[[Image:2jbj.png|left|200px]]
 
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==membrane-bound glutamate carboxypeptidase II (GCPII) in complex with 2-PMPA (2-phosphonoMethyl-pentanedioic acid)==
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The line below this paragraph, containing "STRUCTURE_2jbj", creates the "Structure Box" on the page.
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<StructureSection load='2jbj' size='340' side='right'caption='[[2jbj]], [[Resolution|resolution]] 2.19&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2jbj]] 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=2JBJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JBJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.19&#8491;</td></tr>
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<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=G88:(2S)-2-(PHOSPHONOMETHYL)PENTANEDIOIC+ACID'>G88</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>
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{{STRUCTURE_2jbj| PDB=2jbj | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jbj OCA], [https://pdbe.org/2jbj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jbj RCSB], [https://www.ebi.ac.uk/pdbsum/2jbj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jbj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jb/2jbj_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jbj ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Human glutamate carboxypeptidase II (GCPII) occurs in the central nervous system as well as in human prostate (where it is called prostate-specific membrane antigen; PSMA). Inhibitors of the enzyme have been shown to provide neuroprotection, but may also be useful for the detection, imaging and treatment of prostate cancer. Crystal structures were determined of the extracellular part of GCPII (amino-acid residues 44-750) in complex with two potent inhibitors, quisqualate and 2-PMPA (the strongest GCPII inhibitor to date), at resolutions of 3.0 and 2.2 A, respectively. In addition, models were constructed for binding of the inhibitors willardiine, homoibotenate, L-2-amino-4-phosphonobutanoic acid and L-serine-O-sulfate to the S1' site of the enzyme. The common denominator for high-affinity binding to the S1' site is the formation of two strong salt bridges.
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===MEMBRANE-BOUND GLUTAMATE CARBOXYPEPTIDASE II (GCPII) IN COMPLEX WITH 2-PMPA (2-PHOSPHONOMETHYL-PENTANEDIOIC ACID)===
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Human glutamate carboxypeptidase II inhibition: structures of GCPII in complex with two potent inhibitors, quisqualate and 2-PMPA.,Mesters JR, Henning K, Hilgenfeld R Acta Crystallogr D Biol Crystallogr. 2007 Apr;63(Pt 4):508-13. Epub 2007, Mar 16. PMID:17372356<ref>PMID:17372356</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2jbj" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_17372356}}, adds the Publication Abstract to the page
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*[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 17372356 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17372356}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[2jbj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JBJ OCA].
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==Reference==
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<ref group="xtra">PMID:17372356</ref><ref group="xtra">PMID:16467855</ref><references group="xtra"/>
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[[Category: Glutamate carboxypeptidase II]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Henning, K.]]
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[[Category: Large Structures]]
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[[Category: Hilgenfeld, R.]]
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[[Category: Henning K]]
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[[Category: Mesters, J R.]]
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[[Category: Hilgenfeld R]]
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[[Category: Alternative splicing]]
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[[Category: Mesters JR]]
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[[Category: Antigen]]
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[[Category: Carboxypeptidase]]
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[[Category: Dipeptidase]]
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[[Category: Glycoprotein]]
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[[Category: Hydrolase]]
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[[Category: Membrane]]
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[[Category: Metal- binding]]
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[[Category: Metal-binding]]
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[[Category: Metalloprotease]]
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[[Category: Multifunctional enzyme]]
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[[Category: Naaladase]]
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[[Category: Neurodegenerative disease]]
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[[Category: Peptidase]]
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[[Category: Polymorphism]]
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[[Category: Prostate cancer]]
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[[Category: Protease]]
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[[Category: Psma]]
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[[Category: Signal-anchor]]
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[[Category: Transmembrane]]
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[[Category: Zinc]]
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Current revision

membrane-bound glutamate carboxypeptidase II (GCPII) in complex with 2-PMPA (2-phosphonoMethyl-pentanedioic acid)

PDB ID 2jbj

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