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OJBTM
Online Journal of Bioinformatics ©
Volume 11 (2): 264-281, 2010
Predicted 3D structure, active
site and ligand docking of serine acetyltransferase,
a drug target for Entamoeba histolytica
Subhash Mohan Agarwal* (PhD), Dhwani
Raghav (M.Sc.) and Akshita
Kumar (B.Tech)
Bioinformatics Division, Institute of Cytology and Preventive
Oncology, Uttar Pradesh
ABSTRACT
Agarwal SM, Raghav D, Kumar A, Predicted 3D structure, active site and
ligand docking of serine acetyltransferase, a drug target for Entamoeba histolytica Online J Bioinformatics. 11 (2): 264-281, 2010. Serine acetyltransferase (SATase)
is part of the biosynthetic pathway of E.
histolytica, an enteric parasite that causes
amoebic colitis. The end product, cysteine is an important metabolite for the
survival of E. Histolitica, thus SATase
has become a target for drug development. A 3D-homology model of EhSATase, active site and predicted interactions between
the protein and cysteine, the natural inhibitor are described herein. EhSATase was characterized by unique insertions in an a-helical conformation and an extended loop between b-strand 7 and 8, giving rise to potential significant structural
differences. This structure knowledge may be useful for designing ehSATase inhibitors.
Keywords: Serine
acetyltransferase; Homology modeling; Entamoeba
histolytica; Docking; Amoebiasis
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