1cvi

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(New page: 200px<br /> <applet load="1cvi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cvi, resolution 3.20&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1cvi.gif|left|200px]]<br />
 
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<applet load="1cvi" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cvi, resolution 3.20&Aring;" />
 
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'''CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE==
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BACKGROUND: Prostatic acid phosphatase (hPAP) is a major product of the, human prostate gland, yet its physiological substrate remains unknown., METHODS: Human PAP, purified from semen, was crystallized using, polyethylene glycol as the precipitant and its crystal structure was, determined using X-ray diffraction. The structure was refined at 3.1 A, resolution to R = 16% and R(free) = 27%. RESULTS: The structure of hPAP is, similar to that of other known histidine phosphatases, and the positions, of its catalytic residues are conserved. N-linked carbohydrates are, present at each of the possible glycosylation sites. It appears that, high-mannose chains are attached to Asn 62 and Asp 301, while complex, chains are at Asn 188. CONCLUSIONS: The similarity of the, three-dimensional structures of rat PAP and human PAP indicates that the, mechanistic analyses of the catalytic mechanism proposed for the rat, enzyme should be extended to the human enzyme without reservations. The, crystallographic data allowed the correlation of attachment sites of, N-linked carbohydrate chains with a given carbohydrate type. The, carbohydrates of the protein produced in the prostate cells and in the, baculovirus expression system appear to differ at the site of complex, carbohydrates attachment.
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<StructureSection load='1cvi' size='340' side='right'caption='[[1cvi]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1cvi]] is a 4 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=1CVI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CVI 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]] 3.2&#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=FUC:ALPHA-L-FUCOSE'>FUC</scene>, <scene name='pdbligand=GLY:GLYCINE'>GLY</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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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=1cvi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cvi OCA], [https://pdbe.org/1cvi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cvi RCSB], [https://www.ebi.ac.uk/pdbsum/1cvi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cvi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PPAP_HUMAN PPAP_HUMAN] A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins. Has lipid phosphatase activity and inactivates lysophosphatidic acid in seminal plasma.<ref>PMID:15280042</ref> <ref>PMID:18083097</ref> <ref>PMID:19403677</ref> <ref>PMID:20498373</ref> Isoform 2: the cellular form also has ecto-5'-nucleotidase activity in dorsal root ganglion (DRG) neurons. Generates adenosine from AMP which acts as a pain suppressor. Acts as a tumor suppressor of prostate cancer through dephosphorylation of ERBB2 and deactivation of MAPK-mediated signaling.<ref>PMID:15280042</ref> <ref>PMID:18083097</ref> <ref>PMID:19403677</ref> <ref>PMID:20498373</ref>
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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/cv/1cvi_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=1cvi 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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BACKGROUND: Prostatic acid phosphatase (hPAP) is a major product of the human prostate gland, yet its physiological substrate remains unknown. METHODS: Human PAP, purified from semen, was crystallized using polyethylene glycol as the precipitant and its crystal structure was determined using X-ray diffraction. The structure was refined at 3.1 A resolution to R = 16% and R(free) = 27%. RESULTS: The structure of hPAP is similar to that of other known histidine phosphatases, and the positions of its catalytic residues are conserved. N-linked carbohydrates are present at each of the possible glycosylation sites. It appears that high-mannose chains are attached to Asn 62 and Asp 301, while complex chains are at Asn 188. CONCLUSIONS: The similarity of the three-dimensional structures of rat PAP and human PAP indicates that the mechanistic analyses of the catalytic mechanism proposed for the rat enzyme should be extended to the human enzyme without reservations. The crystallographic data allowed the correlation of attachment sites of N-linked carbohydrate chains with a given carbohydrate type. The carbohydrates of the protein produced in the prostate cells and in the baculovirus expression system appear to differ at the site of complex carbohydrates attachment.
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==About this Structure==
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Crystal structure of human prostatic acid phosphatase .,Jakob CG, Lewinski K, Kuciel R, Ostrowski W, Lebioda L Prostate. 2000 Feb 15;42(3):211-8. PMID:10639192<ref>PMID:10639192</ref>
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1CVI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and GLY as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acid_phosphatase Acid phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.2 3.1.3.2] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1CVI OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of human prostatic acid phosphatase ., Jakob CG, Lewinski K, Kuciel R, Ostrowski W, Lebioda L, Prostate. 2000 Feb 15;42(3):211-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10639192 10639192]
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</div>
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[[Category: Acid phosphatase]]
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<div class="pdbe-citations 1cvi" style="background-color:#fffaf0;"></div>
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[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Jakob, C.G.]]
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[[Category: Kuciel, R.]]
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[[Category: Lebioda, L.]]
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[[Category: Lewinski, K.]]
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[[Category: Ostrowski, W.]]
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[[Category: GLY]]
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[[Category: NAG]]
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[[Category: acid phosphatase]]
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[[Category: inhibition]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:25:43 2007''
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==See Also==
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*[[Acid phosphatase 3D structures|Acid phosphatase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Jakob CG]]
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[[Category: Kuciel R]]
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[[Category: Lebioda L]]
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[[Category: Lewinski K]]
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[[Category: Ostrowski W]]

Current revision

CRYSTAL STRUCTURE OF HUMAN PROSTATIC ACID PHOSPHATASE

PDB ID 1cvi

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