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OJBTM
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.
ABSTRACT
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.
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