Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase.

@article{McCallum2000LigandinducedCI,
  title={Ligand-induced changes in the structure and dynamics of a human class Mu glutathione S-transferase.},
  author={Scott McCallum and T. Kevin Hitchens and Christian Torborg and Gordon S. Rule},
  journal={Biochemistry},
  year={2000},
  volume={39 25},
  pages={
          7343-56
        }
}
Glutathione transferases are detoxification enzymes that catalyze the addition of glutathione (GSH) to a wide variety of hydrophobic compounds. Although this group of enzymes has been extensively characterized by crystallographic studies, little is known about their dynamic properties. This study investigates the role of protein dynamics in the mechanism of a human class mu enzyme (GSTM2-2) by characterizing the motional properties of the unliganded enzyme, the enzyme-substrate (GSH) complex… 
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