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- W3012404094 abstract "The widespread emergence of antibiotic resistance in pathogens necessitates the development of antibacterial agents inhibiting underexplored targets in bacterial metabolism. One such target is phospho-MurNAc-pentapeptide translocase (MraY), an essential integral membrane enzyme that catalyzes the first committed step of peptidoglycan biosynthesis. MraY has long been considered a promising candidate for antibiotic development in part because it is the target of five classes of naturally occurring nucleoside inhibitors with potent in vivo and in vitro antibacterial activity. Although these inhibitors each have a nucleoside moiety, they vary dramatically in their core structures, and they have different activity properties. Until recently, the structural basis of MraY inhibition was poorly understood. Several recent structures of MraY and its human paralog, GlcNAc-1-P-transferase, have provided insights into MraY inhibition that are consistent with known inhibitor activity data and can inform rational drug design for this important antibiotic target." @default.
- W3012404094 created "2020-03-23" @default.
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- W3012404094 date "2020-08-01" @default.
- W3012404094 modified "2023-10-17" @default.
- W3012404094 title "Structures of Bacterial MraY and Human GPT Provide Insights into Rational Antibiotic Design" @default.
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- W3012404094 doi "https://doi.org/10.1016/j.jmb.2020.03.017" @default.
- W3012404094 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/8351759" @default.
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