title: Binding and enantiomeric selectivity of threonyl-tRNA synthetase.
abstract: A combination of MD simulations and free energy calculations have been used to propose a new model for the binding of amino acids to threonyl-tRNA-synthetase which not only yields a stable binding mode for l-Ser but also can explain the mechanism by which the editing domains of aminoacyl-tRNA-synthetases are enantiomeric selective preferentially binding d-amino acids.
authors.affiliation: School of Chemistry and Molecular Biosciences, University of Queensland, St. Lucia, QLD 4072, Australia.
authors.forename: Alpeshkumar K
authors.initials: AK
authors.lastname: Malde
authors.forename: Alan E
authors.initials: AE
authors.lastname: Mark
mesh_terms: D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D003198:Computer Simulation; D008958:Models, Molecular; D011485:Protein Binding; D012694:Serine / Q000737:chemistry / Q000378:metabolism; D013237:Stereoisomerism; D013816:Thermodynamics; D013914:Threonine-tRNA Ligase / Q000737:chemistry* / Q000378:metabolism
chemical_list: D000596:Amino Acids; D012694:Serine; D013914:Threonine-tRNA Ligase