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Current Topics in Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 1568-0266
ISSN (Online): 1873-4294

FtsZ: A Novel Target for Tuberculosis Drug Discovery

Author(s): Qing Huang, Peter J. Tonge, Richard A. Slayden, Teruo Kirikae and Iwao Ojima

Volume 7, Issue 5, 2007

Page: [527 - 543] Pages: 17

DOI: 10.2174/156802607780059790

Price: $65

Abstract

The emergence of multi-drug resistant Mycobacterium tuberculosis (Mtb) strains has made many of the currently available anti-TB drugs ineffective. Accordingly there is a pressing need to identify new drug targets. FtsZ, a bacterial tubulin homologue, is an essential cell division protein that polymerizes in a GTP-dependent manner, forming a highly dynamic cytokinetic ring, designated as the Z ring, at the septum site. Following recruitment of other cell division proteins, the Z ring contracts, resulting in closure of the septum and then formation of two daughter cells. Since inactivation of FtsZ or alteration of FtsZ assembly results in the inhibition of Z ring and septum formation, FtsZ is a very promising target for new antimicrobial drug development. This review describes the function and dynamic behaviors of FtsZ, its homology to tubulin, and recent development of FtsZ inhibitors as potential anti-TB agents.

Keywords: FtsZ, tubulin, GTPase, homology, GTP hydrolysis, polymerization, dynamics, inhibitor

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