Faculty Mentor

Dr. Yao Houndonougbo, Assistant Professor, Department of Chemistry and Biochemistry (yhoundonoug@ewu.edu)

Document Type

Poster

Publication Date

Spring 5-18-2020

Department

Chemistry and Biochemistry

Abstract

Inosine Triphosphatase (ITPA) is an enzymatic molecule that works to prevent the amassed of an intermediate in the formation of purine nucleotides, Inosine Triphosphate (ITP). DNA consists of purine nucleotides, and its metabolic pathway includes the formation of this intermediate. Overpopulation of ITP causes mutations of DNA leading to cancers, increased Inosine levels in DNA and other immunodeficiencies. In order to regulate the ITP concentration, ITPA binds ITP creating a substrate/enzyme complex. In this study, we used computational docking to explore bound conformation and energy of the binding of ITP to ITPA protein. The docking results reveal how ITPA and ITP bind together. The root-mean-square-deviation, rmsd, is computed to analyze the similarity of the docked structures. The binding free energies using the intermolecular energy and the torsion entropy penalty. The significance of this research study is to understand the mechanism of ITPA binding. This is important because it could help in the potential prevention of life-threatening diseases.

Creative Commons License

Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License
This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 4.0 License.

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