HOMOLOGY MODELING OF GLUTAMINASE FREE L-ASPARAGINASE FROM FUSARIUM SOLANI CLR-36

Abstract

This study was aimed to predict the 3D model of L-asparaginase from F. solani CLR-36 along with the prediction of the protein active site and evaluation of the L-asparagine-ligand binding with the protein by protein docking studies. MODELLER9.21 was used to generate the 3D model of L-asparaginase (GenBank: MN166289.1) from F. solani CLR- 36. “Crystal structure of the Asn-bound guinea pig L-asparaginase 1 catalytic domain active site mutant T19A” (PDB id: 5DNC), was used as template to build the model. The built model was validated by PROCHECK software. To predict the active site, BLAST (Basic Local Alignment Search Tool of NCBI) for similarity with Conserved Domain Database (CDD) of NCBI was used, and molecular docking study was carried out using AutoDock Tools. 3D Protein Structure was predicted and the Ramachandran plot of the protein model generated showed 86.1% residues in most favored region indicating the reliability of the model. The protein active sites were evaluated and Docking of L-asparaginase was performed with L-asparagine. The docking result showed that the interactions were occurring at the active site with good binding energy (-6.85kcal/mol) indicating that ligand L-asparagine will show good activity with the target protein-Lasparaginase. This study provides base line information on structural and functional features of L-asparaginase from F. solani CLR-36 with its L-asparagine-ligand which could be useful in the designing of alternative useful drug in the chemotherapy of ALL.