Structure of human PNP complexed with ligands

被引:45
作者
Canduri, F
Silva, RG
dos Santos, DM
Palma, MS
Basso, LA
Santos, DS [1 ]
de Azevedo, WF
机构
[1] Univ Fed Rio Grande do Sul, Dept Biol Mol & Biotecnol, Rede Brasileira Pesquisas TB, BR-91501970 Porto Alegre, RS, Brazil
[2] UNESP, Dept Fis, Programa Posgrad Biofis Mol, BR-15054000 Sao Jose Do Rio Preto, SP, Brazil
[3] Inst Butantan, Ctr Appl Toxinol, BR-05503900 Sao Paulo, Brazil
[4] UNESP, Dept Biol, Inst Biosci, CEIS,Lab Struct Biol & Zoochem, BR-13506900 Rio Claro, SP, Brazil
[5] Pontificia Univ Catolica Rio Grande do Sul, Ctr Pesquisas Biol Mol & Func, BR-90619900 Porto Alegre, RS, Brazil
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2005年 / 61卷
关键词
D O I
10.1107/S0907444905005421
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Purine nucleoside phosphorylase (PNP) is a key enzyme in the purine-salvage pathway, which allows cells to utilize preformed bases and nucleosides in order to synthesize nucleotides. PNP is specific for purine nucleosides in the beta-configuration and exhibits a strong preference for purines containing a 6-keto group and ribosyl-containing nucleosides relative to the corresponding analogues. PNP was crystallized in complex with ligands and data collection was performed using synchrotron radiation. This work reports the structure of human PNP in complex with guanosine (at 2.80 angstrom resolution), 3' deoxyguanosine (at 2.86 angstrom resolution) and 8-azaguanine (at 2.85 angstrom resolution). These structures were compared with the PNP-guanine, PNP-inosine and PNP-immucillin-H complexes solved previously.
引用
收藏
页码:856 / 862
页数:7
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