| Literature DB >> 27284850 |
Dulal Panda1, Dipanwita Bhattacharya1, Quanqing Helen Gao2, Pratik M Oza2, H-Y Jennifer Lin2, Bryson Hawkins2, David E Hibbs2, Paul W Groundwater2.
Abstract
Filamenting temperature-sensitive mutant Z (FtsZ), an essential cell division protein in bacteria, has recently emerged as an important and exploitable antibacterial target. Cytokinesis in bacteria is regulated by the assembly dynamics of this protein, which is ubiquitously present in eubacteria. The perturbation of FtsZ assembly has been found to have a deleterious effect on the cytokinetic machinery and, in turn, upon cell survival. FtsZ is highly conserved among prokaryotes, offering the possibility of broad-spectrum antibacterial agents, while its limited sequence homology with tubulin (an essential protein in eukaryotic mitosis) offers the possibility of selective toxicity. This review aims to summarize current knowledge regarding the mechanism of action of FtsZ, and to highlight existing attempts toward the development of clinically useful inhibitors.Entities:
Keywords: FtsZ; GTP; Z-ring; cytokinesis; inhibitors; polymerization; tubulin
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Year: 2016 PMID: 27284850 DOI: 10.4155/fmc-2016-0041
Source DB: PubMed Journal: Future Med Chem ISSN: 1756-8919 Impact factor: 3.808