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- | [[Image:1v45.gif|left|200px]] | |
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- | {{Structure
| + | ==Crystal Structure of human PNP complexed with 3-deoxyguanosine== |
- | |PDB= 1v45 |SIZE=350|CAPTION= <scene name='initialview01'>1v45</scene>, resolution 2.86Å
| + | <StructureSection load='1v45' size='340' side='right'caption='[[1v45]], [[Resolution|resolution]] 2.86Å' scene=''> |
- | |SITE=
| + | == Structural highlights == |
- | |LIGAND= <scene name='pdbligand=3DG:9-(3-DEOXY-BETA-D-RIBOFURANOSYL)GUANINE'>3DG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | <table><tr><td colspan='2'>[[1v45]] 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=1V45 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1V45 FirstGlance]. <br> |
- | |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>
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.86Å</td></tr> |
- | |GENE=
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3DG:9-(3-DEOXY-BETA-D-RIBOFURANOSYL)GUANINE'>3DG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
- | |DOMAIN=
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1v45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v45 OCA], [https://pdbe.org/1v45 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1v45 RCSB], [https://www.ebi.ac.uk/pdbsum/1v45 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1v45 ProSAT]</span></td></tr> |
- | |RELATEDENTRY=[[1v3q|1V3Q]], [[1v41|1V41]]
| + | </table> |
- | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1v45 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1v45 OCA], [http://www.ebi.ac.uk/pdbsum/1v45 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1v45 RCSB]</span>
| + | == Disease == |
- | }}
| + | [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> |
| + | == Function == |
| + | [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> |
| + | == Evolutionary Conservation == |
| + | [[Image:Consurf_key_small.gif|200px|right]] |
| + | Check<jmol> |
| + | <jmolCheckbox> |
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/v4/1v45_consurf.spt"</scriptWhenChecked> |
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> |
| + | <text>to colour the structure by Evolutionary Conservation</text> |
| + | </jmolCheckbox> |
| + | </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=1v45 ConSurf]. |
| + | <div style="clear:both"></div> |
| + | <div style="background-color:#fffaf0;"> |
| + | == Publication Abstract from PubMed == |
| + | Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine-salvage pathway, which allows cells to utilize preformed bases and nucleosides in order to synthesize nucleotides. PNP is specific for purine nucleosides in the beta-configuration and exhibits a strong preference for purines containing a 6-keto group and ribosyl-containing nucleosides relative to the corresponding analogues. PNP was crystallized in complex with ligands and data collection was performed using synchrotron radiation. This work reports the structure of human PNP in complex with guanosine (at 2.80 A resolution), 3'-deoxyguanosine (at 2.86 A resolution) and 8-azaguanine (at 2.85 A resolution). These structures were compared with the PNP-guanine, PNP-inosine and PNP-immucillin-H complexes solved previously. |
| | | |
- | '''Crystal Structure of human PNP complexed with 3-deoxyguanosine'''
| + | Structure of human PNP complexed with ligands.,Canduri F, Silva RG, dos Santos DM, Palma MS, Basso LA, Santos DS, de Azevedo WF Jr Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):856-62. Epub 2005, Jun 24. PMID:15983407<ref>PMID:15983407</ref> |
| | | |
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| + | </div> |
| + | <div class="pdbe-citations 1v45" style="background-color:#fffaf0;"></div> |
| | | |
- | ==Overview== | + | ==See Also== |
- | Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine-salvage pathway, which allows cells to utilize preformed bases and nucleosides in order to synthesize nucleotides. PNP is specific for purine nucleosides in the beta-configuration and exhibits a strong preference for purines containing a 6-keto group and ribosyl-containing nucleosides relative to the corresponding analogues. PNP was crystallized in complex with ligands and data collection was performed using synchrotron radiation. This work reports the structure of human PNP in complex with guanosine (at 2.80 A resolution), 3'-deoxyguanosine (at 2.86 A resolution) and 8-azaguanine (at 2.85 A resolution). These structures were compared with the PNP-guanine, PNP-inosine and PNP-immucillin-H complexes solved previously. | + | *[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]] |
- | | + | == References == |
- | ==About this Structure== | + | <references/> |
- | 1V45 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=1V45 OCA].
| + | __TOC__ |
- | | + | </StructureSection> |
- | ==Reference==
| + | |
- | Structure of human PNP complexed with ligands., Canduri F, Silva RG, dos Santos DM, Palma MS, Basso LA, Santos DS, de Azevedo WF Jr, Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):856-62. Epub 2005, Jun 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15983407 15983407]
| + | |
| [[Category: Homo sapiens]] | | [[Category: Homo sapiens]] |
- | [[Category: Purine-nucleoside phosphorylase]] | + | [[Category: Large Structures]] |
- | [[Category: Single protein]]
| + | [[Category: Basso LA]] |
- | [[Category: Basso, L A.]] | + | [[Category: Canduri F]] |
- | [[Category: Canduri, F.]] | + | [[Category: De Azevedo Jr WF]] |
- | [[Category: Jr., W F.De Azevedo.]] | + | [[Category: Dos Santos DM]] |
- | [[Category: Mendes, M A.]] | + | [[Category: Mendes MA]] |
- | [[Category: Palma, M S.]] | + | [[Category: Palma MS]] |
- | [[Category: Santos, D M.Dos.]] | + | [[Category: Santos DS]] |
- | [[Category: Santos, D S.]] | + | [[Category: Silva RG]] |
- | [[Category: Silva, R G.]] | + | |
- | [[Category: crystallography]]
| + | |
- | [[Category: drug design]]
| + | |
- | [[Category: purine nucleoside phosphorylase]]
| + | |
- | [[Category: synchrotron]]
| + | |
- | | + | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:19:13 2008''
| + | |
| Structural highlights
Disease
PNPH_HUMAN Defects in PNP are the cause of purine nucleoside phosphorylase deficiency (PNPD) [MIM:613179. It leads to a severe T-cell immunodeficiency with neurologic disorder in children.[1] [2] [3]
Function
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.[4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine-salvage pathway, which allows cells to utilize preformed bases and nucleosides in order to synthesize nucleotides. PNP is specific for purine nucleosides in the beta-configuration and exhibits a strong preference for purines containing a 6-keto group and ribosyl-containing nucleosides relative to the corresponding analogues. PNP was crystallized in complex with ligands and data collection was performed using synchrotron radiation. This work reports the structure of human PNP in complex with guanosine (at 2.80 A resolution), 3'-deoxyguanosine (at 2.86 A resolution) and 8-azaguanine (at 2.85 A resolution). These structures were compared with the PNP-guanine, PNP-inosine and PNP-immucillin-H complexes solved previously.
Structure of human PNP complexed with ligands.,Canduri F, Silva RG, dos Santos DM, Palma MS, Basso LA, Santos DS, de Azevedo WF Jr Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):856-62. Epub 2005, Jun 24. PMID:15983407[5]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Williams SR, Gekeler V, McIvor RS, Martin DW Jr. A human purine nucleoside phosphorylase deficiency caused by a single base change. J Biol Chem. 1987 Feb 15;262(5):2332-8. PMID:3029074
- ↑ Aust MR, Andrews LG, Barrett MJ, Norby-Slycord CJ, Markert ML. Molecular analysis of mutations in a patient with purine nucleoside phosphorylase deficiency. Am J Hum Genet. 1992 Oct;51(4):763-72. PMID:1384322
- ↑ Pannicke U, Tuchschmid P, Friedrich W, Bartram CR, Schwarz K. Two novel missense and frameshift mutations in exons 5 and 6 of the purine nucleoside phosphorylase (PNP) gene in a severe combined immunodeficiency (SCID) patient. Hum Genet. 1996 Dec;98(6):706-9. PMID:8931706
- ↑ Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr, et al.. Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution. J Biol Chem. 1990 Jan 25;265(3):1812-20. PMID:2104852
- ↑ Canduri F, Silva RG, dos Santos DM, Palma MS, Basso LA, Santos DS, de Azevedo WF Jr. Structure of human PNP complexed with ligands. Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):856-62. Epub 2005, Jun 24. PMID:15983407 doi:http://dx.doi.org/10.1107/S0907444905005421
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