Application of Statistical-Thermal Coupling Analysis to Identify Residue-Residue Interaction Networks that Facilitate Coupled-Domain Dynamics in Aminoacyl-tRNA Synthetases
Lehman, Brent P.
Tadayon, Stephanie N.
Zirbes, Arrianna M.
Johnson, James Michael
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Aminoacyl-tRNA synthetases (ARSs) are multi-domain proteins that catalyze covalent attachment of amino acids to the 3'-end of the cognate tRNA molecules. Long-range domain-domain communications are known to play an important role in the function of ARSs. Earlier studies have demonstrated that the coupling of domain motions is important in mediating long-range inter-domain communication in modular proteins. However, the molecular mechanism of coupled-domain motions and long-range communication in ARSs has remained poorly understood. In the present study, the molecular mechanism underlying the coupled-domain motions in ARSs has been probed.
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