Abstract
Pleiotropic effects of therapeutic statins have been frequently reported. The role of p38 MAP kinase has been advanced. In this paper, atorvastatin (containing a terphenylic system), rosuvastatin and fluvastatin, which are important drugs of the statin class, were docked into the active site of p38 MAP kinase where the selective and highly potent inhibitor SB 203580, a fluoro-phenyl pyridinylimidazole derivative, possessing a terphenylic system, binds. The protein-statin complexes near the ATP binding pocket reinforce the hypothesis of p38 MAP kinase as one possible molecular target for statin drugs.
Keywords: Molecular docking, p38 MAP kinase, Pleiotropic effects, Statins
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