New catalytic mechanism for human purine nucleoside phosphorylase

被引：40

作者：

Canduri, F

Fadel, V

Basso, LA

Palma, MS

Santos, DS ^{[1
]}

de Azevedo, WF

机构：

[1] UNESP, Dept Fis, Programa Posgraduacao Biofis Mol, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil

[2] Inst Butantan, Ctr Appl Toxinol, BR-05503900 Sao Paulo, Brazil

[3] Univ Fed Rio Grande do Sul, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisas TB, BR-91501970 Porto Alegre, RS, Brazil

[4] UNESP, Inst Biosci, Dept Biol, Lab Struct Biol & Zoochem CEIS, BR-13506900 Rio Claro, SP, Brazil

[5] Pontif Univ Catolica Rio Grande Sul, Fac Farm, Inst Pesquisas Biomed, Porto Alegre, RS, Brazil

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 327卷 / 03期

基金：

巴西圣保罗研究基金会;

关键词：

PNP; synchrotron radiation; structure; drug design;

D O I：

10.1016/j.bbrc.2004.12.052

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 Inc. All rights reserved.

引用

收藏

页码：646 / 649

页数：4

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