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Online Journal of Bioinformatics©
Volume 21(1): 69-77, 2020.
In Silico 3D E. coli NAD+-dependent DNA ligase drug targets.
Bashir Akhlaq Akhoon (MSc), Gagan Dhaliwal (MSc),Shishir Kumar Gupta (MSc), Mugdha Srivastava (MSc).
1Department of Bioinformatics, Dolphin college of life Sciences, Punjabi University, India, 2Society for Biological Research & Rural Development, Lucknow, India.
Akhoon BA, Dhaliwal G, Gupta SK, Srivastava M., In Silico E. coli NAD+-dependent DNA ligase drug targetss, Onl J Bioinform., 21(1): 69-77, 2020. We describe a 3D model for substrate binding to ATP-dependent human DNA ligases using E.coli NAD+-ligases as target. We identified structural components of bacterial DNA ligase that block NAD+ to ligase. The 3D model NAD+-dependent DNA ligase in E. coli was determined from half sequence structure by wet lab experiments. Protein-drug docking was performed to detect binding affinity with Quinacrine and virtual derivatives. Candidate ligands screened for binding to the conserved and functionally important surface of adenylation domain of bacterial ligaseA using AutoDock4 software showed that the virtual derivative of the Quinacrine with PubChem compound ID of 18331032 possess high binding affinity towards DNA ligase. We found that virtual derivative of Quinacrine (C21H26ClN3O2) had strongest binding affinity. Drug likeness as predicted by Molinspiration confirmed that this virtual derivative could act as a drug. Absence of toxicity risks as prevailed by Osiris Property Explorer enhance the prospect that this ligand can be sent for clinical trials for In Vivo studies.
Keywords: Drug target, NAD+, DNA Ligase, Computational drug discovery.