Model of the Complex of the Human Glycyl-tRNA Synthetase Anticodon-Binding Domain with IRES I Fragment
- Authors: Nikonov O.S.1, Nemchinova M.S.1, Klyashtornii V.G.1, Nikonova E.Y.1, Garber M.B.1
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Affiliations:
- Institute of Protein Research
- Issue: Vol 52, No 1 (2018)
- Pages: 96-102
- Section: Structural Functional Analysis of Biopolymers and Their Complexes
- URL: https://journals.rcsi.science/0026-8933/article/view/163419
- DOI: https://doi.org/10.1134/S0026893318010144
- ID: 163419
Cite item
Abstract
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.
About the authors
O. S. Nikonov
Institute of Protein Research
Author for correspondence.
Email: alik@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
M. S. Nemchinova
Institute of Protein Research
Email: alik@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
V. G. Klyashtornii
Institute of Protein Research
Email: alik@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
E. Yu. Nikonova
Institute of Protein Research
Email: alik@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
M. B. Garber
Institute of Protein Research
Email: alik@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
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