Paul Homes

TL;DR: X-ray crystal structures of compounds bound into bromodomains of Brd2 and Brd4 elucidate the molecular interactions of binding and explain the precisely defined stereochemistry required for activity.

TL;DR: A crystal structure of moxifloxacin in complex with Acinetobacter baumannii topoisomerase IV now shows the wedge-shaped quinolone stacking between base pairs at the DNA cleavage site and binding conserved residues in theDNA cleavage domain through chelation of a noncatalytic magnesium ion.

TL;DR: The first co-crystal structures of the antibacterial QPT-1 and the anticancer drug etoposide with Staphylococcus aureus DNA gyrase are reported, showing binding at the same sites in the cleaved DNA as the fluoroquinolone moxifloxacin.

TL;DR: The assay represents the first report of a RapidFire mass spectrometry assay for an epigenetics target and employs a short amino acid peptide substrate, corresponding to the first 15 amino acid residues of histone H3, but mutated at two positions to increase assay sensitivity.

TL;DR: The results clearly identify KasA as the biological target of GSK3011724A and validate this enzyme for further drug discovery efforts against tuberculosis, and suggest a different mode of inhibition when compared with other Kas inhibitors of fatty acid biosynthesis in bacteria.