Title : Binding and enantiomeric selectivity of threonyl-tRNA synthetase.

Pub. Date : 2009 Mar 25

PMID : 19292486






2 Functional Relationships(s)
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1 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. Serine threonyl-tRNA synthetase 1 Homo sapiens
2 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. d-amino acids threonyl-tRNA synthetase 1 Homo sapiens