Journal article Open Access

IN SILICO PREDICTION AND DOCKING OF TERTIARY STRUCTURE OF PROTEIN X, MULTIFUNCTIONAL PROTEIN OF HEPATITIS B VIRUS (HBV)

Sharav Desai*, Pooja Tahilramani1, Dhara Patel2, Dhananjay Meshram2, Prachi Patel1

Hepatitis B virus (HBV) infection is a universal health problem and may result in acute, fulminant, chronic hepatitis liver cirrhosis, or hepatocellular carcinoma (HCC). The sequence for Protein X of hepatitis B virus was retrieved from UniProt database ProtParam from ExPAsy server was used to investigate the physicochemical properties of the protein. Homology modeling was carried out using Phyre2 server, and Refinement studies were done with Galaxy web browser.Five models were generated and evaluated by ERRAT, ANOLEA, QMEAN6, and PROCHECK. Antigenicity of the protein was also assessed by Chou & Fasman Beta-Turn Prediction method. Five models were generated, and model 1 was having the greatest quality by the QMEAN6 score with 0367 ERRAT analysis reveals the overall quality of 54054% whereas the initial model was having only 17730% quality The mean force potential energy, as analyzed by ANOLEA, were better compared to the original model. Stereochemical quality estimation by Procheck showed that the refined Model 1 had a reliable structure, and was therefore submitted to the protein model database PyRx with Autodock vina was used to screen the compounds from Drug bank and Protein Data Bank to find the molecules that can bind to the active site between 1 to 142 amino acids.Ten compounds with highest negative energy were selected as lead molecules. Protein X structurally evaluated computational methods can be further be experimentally and clinically investigated to develop as potential drug target in Hepatitis B infection. The steps utilized in the article can also be used to investigate the drug target for other infection.

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