Abstract
Homology model of Leishmania SIR2 shed new light on the ligand binding features of this enzyme. The molecular electrostatic potentials (MESP), the cavity depth analysis, and LmSIR2–hSIRT2 models’ superposition suggested that the nicotinamide binding catalytic domain has several minor but potentially important structural differences. These differences could be exploited for designing antileishmanial compounds.
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