1rct
From Proteopedia
(New page: 200px<br /> <applet load="1rct" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rct, resolution 2.80Å" /> '''Crystal structure o...) |
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| - | [[Image:1rct.gif|left|200px]]<br /> | + | [[Image:1rct.gif|left|200px]]<br /><applet load="1rct" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1rct, resolution 2.80Å" /> | caption="1rct, resolution 2.80Å" /> | ||
'''Crystal structure of Human purine nucleoside phosphorylase complexed with INOSINE'''<br /> | '''Crystal structure of Human purine nucleoside phosphorylase complexed with INOSINE'''<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== | ||
| - | 1RCT 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 NOS 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:// | + | 1RCT 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=NOS:'>NOS</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=1RCT 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: Mendes, M | + | [[Category: Mendes, M A.]] |
| - | [[Category: Palma, M | + | [[Category: Palma, M S.]] |
| - | [[Category: Santos, D | + | [[Category: Santos, D M.dos.]] |
| - | [[Category: Santos, D | + | [[Category: Santos, D S.]] |
| - | [[Category: Silva, R | + | [[Category: Silva, R G.]] |
[[Category: NOS]] | [[Category: NOS]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: synchrotron]] | [[Category: synchrotron]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:28 2008'' |
Revision as of 12:49, 21 February 2008
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Crystal structure of Human purine nucleoside phosphorylase complexed with INOSINE
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
1RCT 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
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