1v3q

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[[Image:1v3q.gif|left|200px]]
 
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{{Structure
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==Structure of human PNP complexed with DDI==
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|PDB= 1v3q |SIZE=350|CAPTION= <scene name='initialview01'>1v3q</scene>, resolution 2.80&Aring;
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<StructureSection load='1v3q' size='340' side='right'caption='[[1v3q]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <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>
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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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|ACTIVITY= <span class='plainlinks'>[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] </span>
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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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|GENE= PNP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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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|DOMAIN=
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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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|RELATEDENTRY=[[1rct|1RCT]], [[1v41|1V41]], [[1v45|1V45]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v3q FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v3q OCA], [http://www.ebi.ac.uk/pdbsum/1v3q PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v3q RCSB]</span>
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== Disease ==
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}}
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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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'''Structure of human PNP complexed with DDI'''
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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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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 1v3q" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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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*[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1V3Q is a [[Single protein]] structure of 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=1V3Q OCA].
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__TOC__
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</StructureSection>
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/14706628 14706628]
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[[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: 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://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:19:06 2008''
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Current revision

Structure of human PNP complexed with DDI

PDB ID 1v3q

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