ArticleJournal of molecular modeling2011
Relationship between mutation of serine residue at 315th position in M. tuberculosis catalase-peroxidase enzyme and Isoniazid susceptibility: an in silico analysis.
Article in Journal of molecular modeling, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 71 citations in OpenAlex.
- Novel hypoxanthine guanine phosphoribosyltransferase gene mutations in Saudi Arabian hyperuricemia patients.BioMed research international · 2014Trial
- Exploring Prediction of Antimicrobial Resistance Based on Protein Solvent Accessibility Variation.Frontiers in genetics · 2021Article
- Identification of Conformational B-cell Epitopes in Diphtheria Toxin at Varying Temperatures Using Molecular Dynamics Simulations.Archives of Razi Institute · 2021Article
- Investigating the pathogenic SNPs in BLM helicase and their biological consequences by computational approach.Scientific reports · 2020Article
- Mutations in catalase-peroxidase KatG from isoniazid resistant Mycobacterium tuberculosis clinical isolates: insights from molecular dynamics simulations.Journal of molecular modeling · 2017Article
- Structure-based design of novel naproxen derivatives targeting monomeric nucleoprotein of Influenza A virus.Journal of biomolecular structure & dynamics · 2015Article
- Mechanistic analysis elucidating the relationship between Lys96 mutation in Mycobacterium tuberculosis pyrazinamidase enzyme and pyrazinamide susceptibility.BMC genomics · 2015Article
- Meta-analysis of the association between APC promoter methylation and colorectal cancer.OncoTargets and therapy · 2015Article
- Identification and analysis of driver missense mutations using rotation forest with feature selection.BioMed research international · 2014Article
- In-silico screening of cancer associated mutation on PLK1 protein and its structural consequences.Journal of molecular modeling · 2013Article
- AKT kinase pathway: a leading target in cancer research.TheScientificWorldJournal · 2013Review
- Cancer associated E17K mutation causes rapid conformational drift in AKT1 pleckstrin homology (PH) domain.PloS one · 2013Article
- In silico screening and molecular dynamics simulation of disease-associated nsSNP in TYRP1 gene and its structural consequences in OCA3.BioMed research international · 2013Article
- In silico prediction of a disease-associated STIL mutant and its affect on the recruitment of centromere protein J (CENPJ).FEBS open bio · 2012Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Remarkable advances have been made in the drug therapy of tuberculosis. However much remains to be learned about the molecular and structural basis of drug resistance in Mycobacterium tuberculosis. It is known that, activation of Isoniazid (INH) is mediated by Mycobacterium tuberculosis catalase-peroxidase (MtBKatG) and mutation at position 315 (serine to threonine) leads to resistance. We have conducted studies on the drug resistance through docking and binding analysis supported by time-scale (∼ 1000 ps) and unrestrained all-atom molecular dynamics simulations of wild and mutant MtBKatG. The study showed conformational changes of binding residues. Mutant (S315T) showed high docking score and INH binding affinity as compared to wild enzyme. In molecular dynamics simulation, mutant enzyme exhibited less structure fluctuation at INH binding residues and more degree of fluctuation at C-terminal domain compared to wild enzyme. Our computational studies and data endorse that MtBKatG mutation (S315T) decrease the flexibility of binding residues and made them rigid by altering the conformational changes, in turn it hampers the INH activity. We ascertain from this work that, this study on structural mechanism of resistance development in Mycobacterium tuberculosis would lead to new therapeutics based on the result obtained in this study.
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