Biomedical Letters

Research article | https://doi.org/10.47262/BL/9.1.20230219

In silico structure prediction and molecular docking analyses to reveal potential binding domain of Hepatitis B virus genotype A2

Samar Shahzadi 1*, Qanta Tahir 1, Muhammad Imran Khan 2, Ali Raza 2, Muhammad Fardeen Khan 3, Sajjad Ahmad Larra 4

1 Department of Bioinformatics, Institute of Biochemistry, Biotechnology and Bioinformatics, The Islamia University of Bahawalpur, Bahawalpur, Pakistan

2 Department of Microbiology and Molecular Genetics, University of Okara, Okara, Pakistan

3 Department of Biotechnology, Institute of Biochemistry, Biotechnology and Bioinformatics, The Islamia University of Bahawalpur, Bahawalpur, Pakistan

4 National Institute for Biotechnology and Genetic Engineering (NIBGE), Faisalabad, Pakistan

Abstract

Hepatitis B Virus (HBV) infects the hepatocytes to cause serious liver diseases. HBeAg regulates the response of immune system to the intracellular capsid act as T-cell tolerogen. The immune response regulation may predispose to chronicity during perinatal infections to prevent the severe liver injuries. Various in silico approaches including comparative modeling, threading approach and ab initio approach were employed for the prediction of 3D structures of the selected protein followed by the validation of the predicted structures through Errat, Procheck and Anolea. The predicted 3D structure of HBeAg revealed overall quality factor of 95.9184%. Interestingly, it was observed that only 1.97% residues were present in outlier region while 98.03% in favored and allowed region. Molecular docking analyses were performed and the attempt was for the identification of novel ligands for HBeAg. The reported compound may regulate the activity and act as regulator of HBeAg. Interestingly, least binding energy of -7.1 Kcal/mol was observed in the reported compound and high binding affinity to predict the binding residues (Asp-51, Phe-53, Val-56, Arg-57, Met-95, Ala-98, Asn-103, Arg-111, Asp-112, Val-115, Val-118 and Asn-119). The function determination of the selected target protein is due to the identification of effective binding sites in protein structures. The reported compound may act as potent molecule and the predicted structure is reliable for the functional studies and structural insights.