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Molecular Modeling of Cathepsin B protein in different Leishmania strains

Author(s): Pawan Kumar Jayaswal | Mukta Rani | Chandra Prakash Yadav | Manas Ranjan Dikhit | Ganesh Chandra Sahoo | Pradeep Das

Journal: Journal of Integrated OMICS
ISSN 2182-0287

Volume: 1;
Issue: 1;
Start page: 115;
Date: 2011;
Original page

Keywords: Cathepsin B | Homology Modeling | Leishmaniasis | Simulation | CatB | Cysteine protease

Cathepsin B like cysteine proteases representing a major component of the lysosomal proteolytic repertoire plays an important role in intracel-lular protein degradation. Comparative models of cathepsin B (CatB) protein of six different Leishmania strains were developed using MOD-ELLER. The modeled three-dimensional (3-D) structure has the correct stereochemistry as gauged from the Ramachandran plot and good 3-D structure compatibility as assessed by PROCHECK and the DOPE score (DS2.1, Accelrys). The modeled proteins were energy minimized and validated using standard dynamic cascade protocol (DS 2.1). Seven different disulfide bonding sites are predicted in CatB protein of Leishma-nia. Two domains were identified and different motifs are present in catB protein of Leishmania like aspargine glycosylation sites, protein ki-nase phosphorylation sites, protein kinase C activation sites and N-myristoylation sites. Considering that cathepsin B is essential for survival of Leishmania, including for virulence to the mammalian host, it may be viewed as an attractive drug target.
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