Dr. Yao Houndonougbo, Professor, Department of Chemistry and Biochemistry
Chemistry and Biochemistry
ITPA is an enzyme that is responsible for maintaining a proper level of nonstandard nucleotides in cells. The enzyme is associated with adverse drug reactions for thiopurine or ribavirin therapy. The prediction of drug interactions sites in ITPA protein is important for modulating ITPA-related drug toxicity. There are a vast number of tools available to predict molecular interactions between receptors and ligands. The methods utilized in this study include computational docking to explore bound conformation and energy in the binding of ITP to ITPA protein. The docking results reveal how well ITPA and ITP bind together in comparison to the native complex. The root-mean-square-deviation, rmsd, is computed to analyze the similarity of the docked structures as well as the binding free energies and ligand efficiencies to rank the structures. The significance of this research study is to understand the mechanism of ITPA binding. The importance of this research pertains to visualizing operative configurations of a protein-ligand complex that will cleanse nucleotide pools and repair damaged DNA.
Mpouli, Aulane F., "Molecular Docking Study of ITPA protein substrate complex" (2020). 2020 McNair Scholar Collection. 4.
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