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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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