1v3q

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(New page: 200px<br /> <applet load="1v3q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v3q, resolution 2.80&Aring;" /> '''Structure of human ...)
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[[Image:1v3q.gif|left|200px]]<br />
 
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<applet load="1v3q" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1v3q, resolution 2.80&Aring;" />
 
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'''Structure of human PNP complexed with DDI'''<br />
 
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==Overview==
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==Structure of human PNP complexed with DDI==
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Human purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme which, plays a key role in the purine salvage pathway, and PNP deficiency in, humans leads to an impairment of T-cell function, usually with no apparent, effect on B-cell function. PNP is highly specific for 6-oxopurine, nucleosides and exhibits negligible activity for 6-aminopurine, nucleosides. The catalytic efficiency for inosine is 350,000-fold greater, than for adenosine. Adenine nucleosides and nucleotides are deaminated by, adenosine deaminase and AMP deaminase to their corresponding inosine, derivatives which, in turn, may be further degraded. Here we report the, crystal structures of human PNP in complex with inosine and, 2('),3(')-dideoxyinosine, refined to 2.8A resolution using synchrotron, radiation. The present structures provide explanation for ligand binding, refine the purine-binding site, and can be used for future inhibitor, design.
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<StructureSection load='1v3q' size='340' side='right'caption='[[1v3q]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1v3q]] 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=1V3Q OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V3Q 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]] 2.8&#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=2DI:9-[(2R,5R)-5-(HYDROXYMETHYL)TETRAHYDROFURAN-2-YL]-1,9-DIHYDRO-6H-PURIN-6-ONE'>2DI</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1v3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v3q OCA], [https://pdbe.org/1v3q PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v3q RCSB], [https://www.ebi.ac.uk/pdbsum/1v3q PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v3q ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/PNPH_HUMAN PNPH_HUMAN] Defects in PNP are the cause of purine nucleoside phosphorylase deficiency (PNPD) [MIM:[https://omim.org/entry/613179 613179]. It leads to a severe T-cell immunodeficiency with neurologic disorder in children.<ref>PMID:3029074</ref> <ref>PMID:1384322</ref> <ref>PMID:8931706</ref>
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== Function ==
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[https://www.uniprot.org/uniprot/PNPH_HUMAN PNPH_HUMAN] The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate.<ref>PMID:2104852</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/v3/1v3q_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1v3q 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 purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme which plays a key role in the purine salvage pathway, and PNP deficiency in humans leads to an impairment of T-cell function, usually with no apparent effect on B-cell function. PNP is highly specific for 6-oxopurine nucleosides and exhibits negligible activity for 6-aminopurine nucleosides. The catalytic efficiency for inosine is 350,000-fold greater than for adenosine. Adenine nucleosides and nucleotides are deaminated by adenosine deaminase and AMP deaminase to their corresponding inosine derivatives which, in turn, may be further degraded. Here we report the crystal structures of human PNP in complex with inosine and 2('),3(')-dideoxyinosine, refined to 2.8A resolution using synchrotron radiation. The present structures provide explanation for ligand binding, refine the purine-binding site, and can be used for future inhibitor design.
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==Disease==
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Structures of human purine nucleoside phosphorylase complexed with inosine and ddI.,Canduri F, dos Santos DM, Silva RG, Mendes MA, Basso LA, Palma MS, de Azevedo WF, Santos DS Biochem Biophys Res Commun. 2004 Jan 23;313(4):907-14. PMID:14706628<ref>PMID:14706628</ref>
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Known diseases associated with this structure: Neutral lipid storage disease with myopathy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=609059 609059]], Nucleoside phosphorylase deficiency, immunodeficiency due to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164050 164050]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1V3Q 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 SO4 and 2DI as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Purine-nucleoside_phosphorylase Purine-nucleoside phosphorylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.1 2.4.2.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1V3Q OCA].
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</div>
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<div class="pdbe-citations 1v3q" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Structures of human purine nucleoside phosphorylase complexed with inosine and ddI., Canduri F, dos Santos DM, Silva RG, Mendes MA, Basso LA, Palma MS, de Azevedo WF, Santos DS, Biochem Biophys Res Commun. 2004 Jan 23;313(4):907-14. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14706628 14706628]
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*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Purine-nucleoside phosphorylase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Basso LA]]
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[[Category: Basso, L.A.]]
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[[Category: Canduri F]]
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[[Category: Canduri, F.]]
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[[Category: Palma MS]]
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[[Category: Jr., W.F.de.Azevedo.]]
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[[Category: Pereira JH]]
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[[Category: Palma, M.S.]]
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[[Category: Santos DS]]
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[[Category: Pereira, J.H.]]
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[[Category: Silva RG]]
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[[Category: Santos, D.M.dos.]]
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[[Category: De Azevedo Jr WF]]
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[[Category: Santos, D.S.]]
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[[Category: Dos Santos DM]]
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[[Category: Silva, R.G.]]
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[[Category: 2DI]]
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[[Category: SO4]]
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[[Category: crystallography]]
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[[Category: ddi]]
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[[Category: drug design]]
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[[Category: purine nucleoside phosphorylase]]
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[[Category: synchrotorn]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:41:07 2007''
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Current revision

Structure of human PNP complexed with DDI

PDB ID 1v3q

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