1v2h
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Purine nucleoside phosphorylase (PNP) catalyzes the phosphorolysis of the | + | 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 and has been submitted to extensive structure-based drug design. More recently, the 3-D structure of human PNP has been refined to 2.3A resolution, which allowed a redefinition of the residues involved in the substrate-binding sites and provided a more reliable model for structure-based design of inhibitors. This work reports crystallographic study of the complex of Human PNP:guanine (HsPNP:Gua) solved at 2.7A resolution using synchrotron radiation. Analysis of the structural differences among the HsPNP:Gua complex, PNP apoenzyme, and HsPNP:immucillin-H provides explanation for inhibitor binding, refines the purine-binding site, and can be used for future inhibitor design. |
==Disease== | ==Disease== | ||
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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: Dias, M | + | [[Category: Dias, M V.Bertacine.]] |
| - | [[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: GUN]] | [[Category: GUN]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: synchrotron]] | [[Category: synchrotron]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:30:48 2008'' |
Revision as of 13:30, 21 February 2008
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Crystal structure of human PNP complexed with guanine
Contents |
Overview
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 and has been submitted to extensive structure-based drug design. More recently, the 3-D structure of human PNP has been refined to 2.3A resolution, which allowed a redefinition of the residues involved in the substrate-binding sites and provided a more reliable model for structure-based design of inhibitors. This work reports crystallographic study of the complex of Human PNP:guanine (HsPNP:Gua) solved at 2.7A resolution using synchrotron radiation. Analysis of the structural differences among the HsPNP:Gua complex, PNP apoenzyme, and HsPNP:immucillin-H provides explanation for inhibitor binding, refines 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
1V2H 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
Crystal structure of human PNP complexed with guanine., de Azevedo WF Jr, Canduri F, dos Santos DM, Pereira JH, Bertacine Dias MV, Silva RG, Mendes MA, Basso LA, Palma MS, Santos DS, Biochem Biophys Res Commun. 2003 Dec 19;312(3):767-72. PMID:14680831
Page seeded by OCA on Thu Feb 21 15:30:48 2008
Categories: Homo sapiens | Purine-nucleoside phosphorylase | Single protein | Basso, L A. | Canduri, F. | Dias, M V.Bertacine. | Jr., W F.De Azevedo. | Palma, M S. | Pereira, J H. | Santos, D M.Dos. | Santos, D S. | Silva, R G. | GUN | SO4 | Crystallography | Drug design | Guanine | Purine nucleoside phosphorylase | Synchrotron
