Crystal structure of human PNP complexed with hypoxanthine and sulfate ion

被引:24
作者
Canduri, F
Fadel, V
Dias, MVB
Basso, LA
Palma, MS
Santos, DS [1 ]
de Azevedo, WF
机构
[1] Univ Fed Rio Grande do Sul, Dept Mol Biol & Biotechnol, BR-91501970 Porto Alegre, RS, Brazil
[2] UNESP, Programa Posgraduacao Biofis Mol, Dept Fis, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
[3] Inst Butantan, Ctr Appl Toxinol, BR-05503900 Sao Paulo, Brazil
[4] UNESP, Lab Struct Biol & Zoochem, CEIS, Dept Biol,Inst Biosci, BR-13506900 Rio Claro, SP, Brazil
[5] Pontificia Univ Catolica Rio Grande do Sul, Ctr Pesquisas Biol Mol & Func, Inst Pesquisas Biomed, BR-90619900 Porto Alegre, RS, Brazil
基金
巴西圣保罗研究基金会;
关键词
PNP; synchrotron radiation; structure; drug design; hypoxanthine;
D O I
10.1016/j.bbrc.2004.11.038
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
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 effects on B-cell function. Human PNP has been submitted to intensive structure-based design of inhibitors, most of them using low-resolution structures of human PNP. Here we report the crystal structure of human PNP in complex with hypoxanthine, refined to 2.6 Angstrom resolution. The intermolecular interaction between ligand and PNP is discussed. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:335 / 338
页数:4
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