1pf7
From Proteopedia
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- | {{STRUCTURE_1pf7| PDB=1pf7 | SCENE= }} | ||
- | ===CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH IMMUCILLIN H=== | ||
- | {{ABSTRACT_PUBMED_13679061}} | ||
- | == | + | ==CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH IMMUCILLIN H== |
- | [[http://www.uniprot.org/uniprot/PNPH_HUMAN PNPH_HUMAN | + | <StructureSection load='1pf7' size='340' side='right'caption='[[1pf7]], [[Resolution|resolution]] 2.60Å' scene=''> |
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1pf7]] 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=1PF7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PF7 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IMH:1,4-DIDEOXY-4-AZA-1-(S)-(9-DEAZAHYPOXANTHIN-9-YL)-D-RIBITOL'>IMH</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
+ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1pf7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pf7 OCA], [https://pdbe.org/1pf7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pf7 RCSB], [https://www.ebi.ac.uk/pdbsum/1pf7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pf7 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == 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/pf/1pf7_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=1pf7 ConSurf]. | ||
+ | <div style="clear:both"></div> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the N-ribosidic bonds of purine nucleosides and deoxynucleosides. PNP is a target for inhibitor development aiming at T-cell immune response modulation. This work reports on the crystallographic study of the complex of human PNP-immucillin-H (HsPNP-ImmH) solved at 2.6A resolution using synchrotron radiation. Immucillin-H (ImmH) inhibits the growth of malignant T-cell lines in the presence of deoxyguanosine without affecting non-T-cell tumor lines. ImmH inhibits activated normal human T cells after antigenic stimulation in vitro. These biological effects of ImmH suggest that this agent may have utility in the treatment of certain human diseases characterized by abnormal T-cell growth or activation. This is the first structural report of human PNP complexed with immucillin-H. The comparison of the complex HsPNP-ImmH with recent crystallographic structures of human PNP explains the high specificity of immucillin-H for human PNP. | ||
- | + | Structural basis for inhibition of human PNP by immucillin-H.,Filgueira de Azevedo W Jr, Canduri F, Marangoni dos Santos D, Pereira JH, Dias MV, Silva RG, Mendes MA, Basso LA, Palma MS, Santos DS Biochem Biophys Res Commun. 2003 Oct 3;309(4):917-22. PMID:13679061<ref>PMID:13679061</ref> | |
- | + | ||
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
+ | <div class="pdbe-citations 1pf7" style="background-color:#fffaf0;"></div> | ||
- | == | + | ==See Also== |
- | + | *[[Purine nucleoside phosphorylase 3D structures|Purine nucleoside phosphorylase 3D structures]] | |
+ | == References == | ||
+ | <references/> | ||
+ | __TOC__ | ||
+ | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: | + | [[Category: Large Structures]] |
- | + | [[Category: Basso LA]] | |
- | [[Category: Basso | + | [[Category: Canduri F]] |
- | [[Category: Canduri | + | [[Category: De Azevedo Jr WF]] |
- | [[Category: | + | [[Category: Dias MVB]] |
- | [[Category: | + | [[Category: Dos Santos DM]] |
- | [[Category: | + | [[Category: Mendes MA]] |
- | + | [[Category: Palma MS]] | |
- | + | [[Category: Pereira JH]] | |
- | + | [[Category: Santos DS]] | |
- | [[Category: | + | [[Category: Silva RG]] |
- | [[Category: | + | |
- | [[Category: | + | |
- | [[Category: | + | |
- | [[Category: | + |
Current revision
CRYSTAL STRUCTURE OF HUMAN PNP COMPLEXED WITH IMMUCILLIN H
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Categories: Homo sapiens | Large Structures | Basso LA | Canduri F | De Azevedo Jr WF | Dias MVB | Dos Santos DM | Mendes MA | Palma MS | Pereira JH | Santos DS | Silva RG