Homology Modeling and Protein-Protein Molecular Docking analyses elucidate the Potential Binding Pockets of ATP7B: A Candidate Wilson’s disease

Abstract

There has been progressive improvement in computational drug design from last decade. Numerous computer aided compounds have been reported against neurodegenerative disorders. Wilson’s disease is a common neurodegenerative disease in humans associated with ATP7B that encodes a transmembrane copper-transporting ATPase which induces the copper export from hepatic cells into bile and supplies copper for the functional synthesis of Ceruloplasmin. Almost, 150 mutations of ATP7B have been identified lead to cause Wilson's disease having symptoms of cancers, loss of memory and postural instability. In this research article, 3D structure of ATP7B was predicted by using comparative modelling approaches. The predicted structures were evaluated by utilizing numerous evaluation tools and 98.50% of overall quality factor was observed for the final selected structure. ATOX1 was predicted as the interacting partner of ATP7B and molecular docking analyses of ATP7B and ATOX1 were conducted by using PatchDock. The least global energy of -35.45 Kcal/mol was observed having the interacting residues in the binding pocket. The reported interacting residues may help to target the specific drug development against ATP7B. This research article can be a major initiative to predict the therapeutic drug targets against Wilson’s disease.