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Biochem Biophys Res Commun. 2005 Feb 18;327(3):646-9.

New catalytic mechanism for human purine nucleoside phosphorylase.

Author information

1
Programa de Pós-graduação em Biofísica Molecular, Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil. canduri@webmail.ibilce.unesp.br

Abstract

Human purine nucleoside phosphorylase has been submitted to intensive structure-based design of inhibitors, most of them using low-resolution structures of human PNP. Recently, several structures of human PNP have been reported, which allowed redefinition of the active site and understanding of the structural basis for inhibition of PNP by acyclovir and immucillin-H. Based on previously solved human PNP structures, we proposed here a new catalytic mechanism for human PNP, which is supported by crystallographic studies and explains previously determined kinetic data.

PMID:
15649395
DOI:
10.1016/j.bbrc.2004.12.052
[Indexed for MEDLINE]

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