Structural highlights
Function
SYTC_HUMAN
Publication Abstract from PubMed
A series of potent and bacteria-selective threonyl-tRNA synthetase (ThrRS) inhibitors have been identified using structure-based drug design. These compounds occupied the substrate binding site of ThrRS and showed excellent binding affinities for all of the bacterial orthologues tested. Some of the compounds displayed greatly improved bacterial selectivity. Key residues responsible for potency and bacteria/human ThrRS selectivity have been identified. Antimicrobial activity has been achieved against wild-type Haemophilus influenzae and efflux-deficient mutants of Escherichia coli and Burkholderia thailandensis.
Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design.,Teng M, Hilgers MT, Cunningham ML, Borchardt A, Locke JB, Abraham S, Haley G, Kwan BP, Hall C, Hough GW, Shaw KJ, Finn J J Med Chem. 2013 Feb 28;56(4):1748-60. doi: 10.1021/jm301756m. Epub 2013 Feb 12. PMID:23362938[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Teng M, Hilgers MT, Cunningham ML, Borchardt A, Locke JB, Abraham S, Haley G, Kwan BP, Hall C, Hough GW, Shaw KJ, Finn J. Identification of bacteria-selective threonyl-tRNA synthetase substrate inhibitors by structure-based design. J Med Chem. 2013 Feb 28;56(4):1748-60. doi: 10.1021/jm301756m. Epub 2013 Feb 12. PMID:23362938 doi:10.1021/jm301756m
