AN INTEGRATIVE IN SILICO CHARACTERIZATION AND DOCKING STUDIES OF Β- ENOLASE: A NOVEL THERAPEUTIC INSIGHT FOR Β- -ENOLASE DEFICIENCY

Abstract

The β-Enolase protein deficiency causes the glycogen storage disease type 13-βEnolase deficiency. An in silico comparative modelling and docking studies were conducted as the structural information about the protein was unavailable in any of the structural databases .The crystal structure of neuron specific enolase (PDBID: 1TE6, Chain A) was selected as best template and it was modelled by MODELLER 9v7. The PROCHECK analysis accounted for 92% of the residues in the most favored region of Ramachandran plot and structure quality factor is 95.30%. The protein showed 0.1 Ao RMSD and it is submitted to Protein Model Database with ID: PM0076547. The docking studies with selected ligands were conducted and concluded that Nonaethylene glycol was the best ligand of choice with Etotal– 95.82. Hence, with the reliable β-Enolase Protein model and the docking studies, it infers that this inhibitor can be used as a potential drug candidate against β-Enolase protein.