title: Comparative protein modeling and surface analysis of Leishmania sirtuin: A potential target for antileishmanial drug discovery.
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.
authors.affiliation: Centre of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research, Sector 67, S. A. S. Nagar, Punjab 160062, India.
authors.forename: Rameshwar U
authors.initials: RU
authors.lastname: Kadam
authors.forename: V M
authors.initials: VM
authors.lastname: Kiran
authors.forename: Nilanjan
authors.initials: N
authors.lastname: Roy
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D017124:Conserved Sequence; D006801:Humans; D007891:Leishmania / Q000201:enzymology*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D037761:Sirtuins / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D055672:Static Electricity; D040681:Structural Homology, Protein; D014344:Trypanocidal Agents / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D014344:Trypanocidal Agents; D037761:Sirtuins