Canduri, F.Fadel, VBasso, L. A.Palma, Mario Sergio [UNESP]Santos, D. S.de Azevedo, W. F.2014-05-202014-05-202005-02-18Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc. Elsevier B.V., v. 327, n. 3, p. 646-649, 2005.0006-291Xhttp://hdl.handle.net/11449/19552Human 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.646-649engPNPsynchrotron radiationStructuredrug designArtigo10.1016/j.bbrc.2004.12.052WOS:000226674800003Acesso restrito28350290616965802901888624506535