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Infectious disease


Mycobacterium tuberculosis probable ATP-dependent protease ATP-binding subunit ClpC1 (ClpC1)

In vitro studies identified ClpC1 as the target of antituberculosis compound cyclomarin A (CymA), which could guide the design of new ClpC1 inhibitors to treat tuberculosis. CymA has activity against both replicating and nonreplicating tuberculosis, but the 848-amino-acid protein has poor pharmacokinetics. Cocrystallization of CymA in complex with ClpC1 showed that the compound bound the N-terminal domain of ClpC1. Next steps include designing ClpC1 inhibitors with improved therapeutic properties.

SciBX 6(39); doi:10.1038/scibx.2013.1100
Published online Oct. 10, 2013

Findings unpatented; licensing status not applicable

Vasudevan, D. et al. J. Biol. Chem.; published online Sept. 10, 2013;
Contact: Christian G. Noble, Novartis Institute for Tropical Diseases, Chromos, Singapore