曼氏血吸虫嘌呤核苷磷酸化酶的结构生物信息学研究
Structural bioinformatics study of PNP from Schistosoma mansoni.
作者信息
da Silveira Nelson José Freitas, Uchôa Hugo Brandão, Canduri Fernanda, Pereira José Henrique, Camera João Carlos, Basso Luiz Augusto, Palma Mário Sergio, Santos Diógenes Santiago, de Azevedo Walter Filgueira
机构信息
Department of Physics, UNESP, São José do Rio Preto, SP 15054-000, Brazil.
出版信息
Biochem Biophys Res Commun. 2004 Sep 10;322(1):100-4. doi: 10.1016/j.bbrc.2004.07.088.
The parasite Schistosoma mansoni lacks the de novo pathway for purine biosynthesis and depends on salvage pathways for its purine requirements. Schistosomiasis is endemic in 76 countries and territories and amongst the parasitic diseases ranks second after malaria in terms of social and economic impact and public health importance. The PNP is an attractive target for drug design and it has been submitted to extensive structure-based design. The atomic coordinates of the complex of human PNP with inosine were used as template for starting the modeling of PNP from S. mansoni complexed with inosine. Here we describe the model for the complex SmPNP-inosine and correlate the structure with differences in the affinity for inosine presented by human and S. mansoni PNPs.
曼氏血吸虫这种寄生虫缺乏嘌呤生物合成的从头合成途径，其嘌呤需求依赖于补救途径。血吸虫病在76个国家和地区流行，在寄生虫病中，就社会和经济影响以及公共卫生重要性而言，仅次于疟疾排名第二。嘌呤核苷磷酸化酶是药物设计的一个有吸引力的靶点，并且已经进行了广泛的基于结构的设计。人嘌呤核苷磷酸化酶与肌苷复合物的原子坐标被用作模板，以启动曼氏血吸虫嘌呤核苷磷酸化酶与肌苷复合物的建模。在此，我们描述了曼氏血吸虫嘌呤核苷磷酸化酶-肌苷复合物的模型，并将该结构与人和曼氏血吸虫嘌呤核苷磷酸化酶对肌苷亲和力的差异相关联。
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