1v3q
From Proteopedia
(New page: 200px<br /> <applet load="1v3q" size="450" color="white" frame="true" align="right" spinBox="true" caption="1v3q, resolution 2.80Å" /> '''Structure of human ...) |
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| - | [[Image:1v3q.gif|left|200px]]<br /> | + | [[Image:1v3q.gif|left|200px]]<br /><applet load="1v3q" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1v3q, resolution 2.80Å" /> | caption="1v3q, resolution 2.80Å" /> | ||
'''Structure of human PNP complexed with DDI'''<br /> | '''Structure of human PNP complexed with DDI'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human purine nucleoside phosphorylase (PNP) is a ubiquitous enzyme which | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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:// | + | 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=2DI:'>2DI</scene> 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1V3Q OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Purine-nucleoside phosphorylase]] | [[Category: Purine-nucleoside phosphorylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Basso, L | + | [[Category: Basso, L A.]] |
[[Category: Canduri, F.]] | [[Category: Canduri, F.]] | ||
| - | [[Category: Jr., W | + | [[Category: Jr., W F.de Azevedo.]] |
| - | [[Category: Palma, M | + | [[Category: Palma, M S.]] |
| - | [[Category: Pereira, J | + | [[Category: Pereira, J H.]] |
| - | [[Category: Santos, D | + | [[Category: Santos, D M.dos.]] |
| - | [[Category: Santos, D | + | [[Category: Santos, D S.]] |
| - | [[Category: Silva, R | + | [[Category: Silva, R G.]] |
[[Category: 2DI]] | [[Category: 2DI]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: synchrotorn]] | [[Category: synchrotorn]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:31:10 2008'' |
Revision as of 13:31, 21 February 2008
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Structure of human PNP complexed with DDI
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Neutral lipid storage disease with myopathy OMIM:[609059], Nucleoside phosphorylase deficiency, immunodeficiency due to OMIM:[164050]
About this Structure
1V3Q is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Purine-nucleoside phosphorylase, with EC number 2.4.2.1 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:31:10 2008
Categories: Homo sapiens | Purine-nucleoside phosphorylase | Single protein | Basso, L A. | Canduri, F. | Jr., W F.de Azevedo. | Palma, M S. | Pereira, J H. | Santos, D M.dos. | Santos, D S. | Silva, R G. | 2DI | SO4 | Crystallography | Ddi | Drug design | Purine nucleoside phosphorylase | Synchrotorn
