Biotechnology and Biosciences Research Group, Faculty of Chemical Sciences and Engineering, Autonomous University of Baja California, Tijuana 22390, Mexico.
Genes (Basel). 2021 Jul 28;12(8):1139. doi: 10.3390/genes12081139.
The target of rapamycin (TOR), also known as FKBP-rapamycin associated protein (FRAP), is a protein kinase belonging to the PIKK (phosphatidylinositol 3-kinase (PI3K)-related kinases) family. TOR kinases are involved in several signaling pathways that control cell growth and proliferation. , the protozoan parasite that causes human amoebiasis, contains two genes encoding TOR-like proteins: FRAP and TOR2. To assess their potential as drug targets to control the cell proliferation of , we studied the structural features of FRAP and TOR2 using a biocomputational approach. The overall results confirmed that both TOR amoebic homologs share structural similarities with functional TOR kinases, and show inherent abilities to form TORC complexes and participate in protein-protein interaction networks. To our knowledge, this study represents the first in silico characterization of the structure-function relationships of FRAP and TOR2.
雷帕霉素靶蛋白（TOR），也称为 FKBP-雷帕霉素相关蛋白（FRAP），是一种属于 PIKK（磷脂酰肌醇 3-激酶（PI3K）相关激酶）家族的蛋白激酶。TOR 激酶参与控制细胞生长和增殖的几种信号通路。引起人类阿米巴病的原生动物寄生虫含有两个编码 TOR 样蛋白的基因：FRAP 和 TOR2。为了评估它们作为控制细胞增殖的药物靶点的潜力，我们使用生物计算方法研究了 FRAP 和 TOR2 的结构特征。总体结果证实，两种 TOR 阿米巴同源物都与功能 TOR 激酶具有结构相似性，并具有形成 TORC 复合物和参与蛋白质-蛋白质相互作用网络的固有能力。据我们所知，这项研究首次在计算机上对 FRAP 和 TOR2 的结构-功能关系进行了描述。
