Canduri Fernanda, Silva Rafael Guimarães, dos Santos Denis Marangoni, Palma Mário Sérgio, Basso Luiz Augusto, Santos Diógenes Santiago, de Azevedo Walter Filgueira
Programa de Pós-Graduação em Biofísica Molecular, Departamento de Física, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
Acta Crystallogr D Biol Crystallogr. 2005 Jul;61(Pt 7):856-62. doi: 10.1107/S0907444905005421. Epub 2005 Jun 24.
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 A resolution), 3'-deoxyguanosine (at 2.86 A resolution) and 8-azaguanine (at 2.85 A resolution). These structures were compared with the PNP-guanine, PNP-inosine and PNP-immucillin-H complexes solved previously.
嘌呤核苷磷酸化酶（PNP）是嘌呤补救途径中的关键酶，该途径使细胞能够利用预先形成的碱基和核苷来合成核苷酸。PNP对β构型的嘌呤核苷具有特异性，相对于相应类似物，它对含有6-酮基的嘌呤和含核糖基的核苷表现出强烈偏好。PNP与配体形成复合物后结晶，并使用同步辐射进行数据收集。这项工作报道了人PNP与鸟苷（分辨率为2.80 Å）、3'-脱氧鸟苷（分辨率为2.86 Å）和8-氮杂鸟嘌呤（分辨率为2.85 Å）形成复合物的结构。将这些结构与先前解析的PNP-鸟嘌呤、PNP-肌苷和PNP-免疫球蛋白-H复合物进行了比较。
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