In silico analysis of heme binding effect on the formation of mouse arginyl-tRNA-protein transferase 1 and protein LIAT1 complex
Keywords:
heme binding, arginyl-tRNA-protein transferase, LIAT1 protein, 3D-modelling, dockingAbstract
Ab initio prediction of mouse arginyl-tRNA-protein transferase 1 (R-transferase, EC 2.3.2.8) and protein LIAT1 structures was performed by I-Tasser server. Molecular docking studies of the protein models revealed that potential heme binding sites didn’t coincide with the sites of interaction with protein partner in both R-transferase and LIAT1 protein. Heme docking to the complex of two proteins showed LIAT1 protein to provide more preferable sites for heme binding than R-transferase. Heme attachment to the cavities in the core of R-transferase involved in catalysis and the alterations of LIAT1 protein conformation could be the additional mechanisms of heme inhibiting action on protein arginylation.
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