1v3q

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spinqualitylabelsall models PDB ID 1v3q Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.80Å
Ligands:	and
Gene:	PNP (Homo sapiens)
Activity:	Purine-nucleoside phosphorylase, with EC number 2.4.2.1
Coordinates:	save as pdb, mmCIF, xml

Structure of human PNP complexed with DDI

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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. 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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