Computational Overview of Mycobacterial Thymidine Monophosphate Kinase.
QSAR
SAR
Tuberculosis
crystal
docking
pharmacophore.
Journal
Current pharmaceutical design
ISSN: 1873-4286
Titre abrégé: Curr Pharm Des
Pays: United Arab Emirates
ID NLM: 9602487
Informations de publication
Date de publication:
2020
2020
Historique:
received:
04
10
2019
accepted:
30
12
2019
pubmed:
4
4
2020
medline:
20
11
2020
entrez:
4
4
2020
Statut:
ppublish
Résumé
Tuberculosis (TB) ranks among the diseases with the highest morbidity rate with significantly high prevalence in developing countries. Globally, tuberculosis poses the most substantial burden of mortality. Further, a partially treated tuberculosis patient is worse than untreated; they may lead to standing out as a critical obstacle to global tuberculosis control. The emergence of multi-drug resistant (MDR) and extremely drug-resistant (XDR) strains, and co-infection of HIV further worsen the situation. The present review article discusses validated targets of the bacterial enzyme thymidine monophosphate kinase (TMPK). TMPKMTB enzyme belongs to the nucleoside monophosphate kinases (NMPKs) family. It is involved in phosphorylation of TMP to TDP, and TDP is phosphorylated to TTP. This review highlights structure elucidation of TMP enzymes and their inhibitors study on TMP scaffold, and it also discusses different techniques; including molecular docking, virtual screening, 3DPharmacophore, QSAR for finding anti-tubercular agents.
Identifiants
pubmed: 32242781
pii: CPD-EPUB-105636
doi: 10.2174/1381612826666200403114152
doi:
Substances chimiques
Antitubercular Agents
0
Nucleoside-Phosphate Kinase
EC 2.7.4.4
dTMP kinase
EC 2.7.4.9
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
1676-1681Informations de copyright
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