Nikonov O S, Nemchinova M S, Klyashtornii V G, Nikonova E Yu, Garber M B
Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.
Mol Biol (Mosk). 2018 Jan-Feb;52(1):112-119.
The currently available structural information is insufficient for a detailed analysis of interactions between human glycyl-tRNA synthetase (GARS) and enterovirus IRESs. At the same time, this information is required in order to understand how this IRES trans-acting factor (ITAF) functions during viral mRNA translation, which is in turn crucial for the development of direct-action antiviral agents. In this paper, a theoretical model of the complex between a cadicivirus A IRES fragment and the anticodon-binding domain of human GARS is constructed using molecular dynamics simulation based on all of the available structural and biochemical data. The proposed model enables the structural interpretation of the previously obtained biochemical data.
目前可获得的结构信息不足以对人甘氨酰 - tRNA合成酶（GARS）与肠道病毒内部核糖体进入位点（IRES）之间的相互作用进行详细分析。与此同时，为了理解这种IRES反式作用因子（ITAF）在病毒mRNA翻译过程中是如何发挥作用的，就需要这些信息，而这反过来对于直接作用抗病毒药物的开发至关重要。在本文中，基于所有可用的结构和生化数据，利用分子动力学模拟构建了杯状病毒A IRES片段与人GARS反密码子结合结构域之间复合物的理论模型。所提出的模型能够对先前获得的生化数据进行结构解释。
