Publication: New catalytic mechanism for human purine nucleoside phosphorylase
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Date
Advisor
Coadvisor
Graduate program
Undergraduate course
Journal Title
Journal ISSN
Volume Title
Publisher
Elsevier B.V.
Type
Article
Access right
Acesso restrito
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. (C) 2004 Elsevier B.V. All rights reserved.
Description
Keywords
PNP, synchrotron radiation, Structure, drug design
Language
English
Citation
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 327, n. 3, p. 646-649, 2005.
