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Exploring the dark side of tertiary and quaternary structure dynamics in MtbFBPaseII.pdf (1.91 MB)

Exploring the dark side of tertiary and quaternary structure dynamics in Mtb FBPaseII

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posted on 2023-10-25, 15:45 authored by Gabriel Luís Cardoso Greco, Natanael Segretti, Celerino Abad-ZapateroCelerino Abad-Zapatero, Farahnaz Movahed ZadehFarahnaz Movahed Zadeh, Mario Hiroyuki Hirata, Elizabeth Igne Ferreira, Glaucio Monteiro Ferreira

Tuberculosis (TB) is a major global cause of mortality, primarily stemming from latent tuberculosis infection (LTBI). Failure to fully treat LTBI can result in drug-resistant forms of TB. Therefore, it is essential to develop novel drugs with unique mechanisms of action to combat TB effectively. One crucial metabolic pathway in Mycobacterium tuberculosis (Mtb), which contributes to TB infection and persistence, is gluconeogenesis. Within this pathway, the enzyme fructose bisphosphatase (FBPase) plays a significant role and is considered a promising target for drug development. By targeting MtbFBPaseII, a specific class of FBPase, researchers have employed molecular dynamics simulations to identify regions capable of binding new drugs, thereby inhibiting the enzyme’s activity and potentially paving the way for the development of effective treatments. 

History

Citation

Greco, G. L. C., Segretti, N., Abad-Zapatero, C., Movahedzadeh, F., Hirata, M. H., Ferreira, E. I.Ferreira, G. M. (n.d.). Exploring the dark side of tertiary and quaternary structure dynamics in Mtb FBPaseII. Journal of Biomolecular Structure and Dynamics, 1-9. https://doi.org/10.1080/07391102.2023.2270528

Publisher

Informa UK Limited

Language

  • en

issn

0739-1102

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