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Structure-Guided Enhancement of Selectivity of Chemical Probe Inhibitors Targeting Bacterial Seryl-tRNA Synthetase. | LitMetric

AI Article Synopsis

  • * The study focused on bacterial seryl-tRNA synthetases and determined their high-resolution X-ray crystal structures with analogues, providing insights for drug design.
  • * Researchers identified small molecule inhibitors that selectively block bacterial seryl-tRNA synthetases effectively while sparing human versions, addressing challenges in targeting bacteria specifically.

Article Abstract

Aminoacyl-tRNA synthetases are ubiquitous and essential enzymes for protein synthesis and also a variety of other metabolic processes, especially in bacterial species. Bacterial aminoacyl-tRNA synthetases represent attractive and validated targets for antimicrobial drug discovery if issues of prokaryotic versus eukaryotic selectivity and antibiotic resistance generation can be addressed. We have determined high-resolution X-ray crystal structures of the and seryl-tRNA synthetases in complex with aminoacyl adenylate analogues and applied a structure-based drug discovery approach to explore and identify a series of small molecule inhibitors that selectively inhibit bacterial seryl-tRNA synthetases with greater than 2 orders of magnitude compared to their human homologue, demonstrating a route to the selective chemical inhibition of these bacterial targets.

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Source
http://dx.doi.org/10.1021/acs.jmedchem.9b01131DOI Listing

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