ArticleJournal of molecular modeling2008
Molecular modeling and dynamics studies of cytidylate kinase from Mycobacterium tuberculosis H37Rv.
Article in Journal of molecular modeling, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 20 citations in OpenAlex.
- Resistance related metabolic pathways for drug target identification in Mycobacterium tuberculosis.BMC bioinformatics · 2016Article
- Insight from the structural molecular model of cytidylate kinase from Mycobacterium tuberculosis.Bioinformation · 2013Article
- Exploring the molecular basis for selective binding of Mycobacterium tuberculosis Asp kinase toward its natural substrates and feedback inhibitors: a docking and molecular dynamics study.Journal of molecular modeling · 2010Article
- Structural studies of shikimate dehydrogenase from Bacillus anthracis complexed with cofactor NADP.Journal of molecular modeling · 2009Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial cytidylate kinase or cytidine monophosphate kinase (CMP kinase) catalyses the phosphoryl transfer from ATP to CMP and dCMP, resulting in the formation nucleoside diphosphates. In eukaryotes, CMP/UMP kinase catalyses the conversion of UMP and CMP to, respectively, UDP and CDP with high efficiency. This work describes for the first time a model of bacterial cytidylate kinase or cytidine monophosphate kinase (CMP kinase) from mycobacterium tuberculosis (MtCMPK). We modeled MtPCMPK in apo form and in complex with cytidine 5'-monophosphate (CMP) to try to determine the structural basis for specificity. Comparative analysis of the model of MtCMPK allowed identification of structural features responsible for ligand affinities. Analysis of the molecular dynamics simulations of these two systems indicates the structural features responsible for the stability of the structure, and may help in the identification of new inhibitors for this enzyme.
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