1v2h

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1v2h, resolution 2.70Å

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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 SO4 and GUN 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

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