Comparative protein modeling and surface analysis of Leishmania sirtuin: A potential target for antileishmanial drug discovery.
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.
Kadam
Rameshwar U
RU
Centre of Pharmacoinformatics, National Institute of Pharmaceutical Education and Research, Sector 67, S. A. S. Nagar, Punjab 160062, India.
Kiran
V M
VM
Roy
Nilanjan
N
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*
D014344:Trypanocidal Agents; D037761:Sirtuins