Structural highlights
Publication Abstract from PubMed
Crystallographic analyses of the VIM-5 metallo-beta-lactamase (MBL) with isoquinoline inhibitors reveal non zinc ion binding modes. Comparison with other MBL-inhibitor structures directed addition of a zinc-binding thiol enabling identification of potent B1 MBL inhibitors. The inhibitors potentiate meropenem activity against clinical isolates harboring MBLs.
Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition.,Li GB, Brem J, Lesniak R, Abboud MI, Lohans CT, Clifton IJ, Yang SY, Jimenez-Castellanos JC, Avison MB, Spencer J, McDonough MA, Schofield CJ Chem Commun (Camb). 2017 May 4. doi: 10.1039/c7cc02394d. PMID:28470248[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Li GB, Brem J, Lesniak R, Abboud MI, Lohans CT, Clifton IJ, Yang SY, Jimenez-Castellanos JC, Avison MB, Spencer J, McDonough MA, Schofield CJ. Crystallographic analyses of isoquinoline complexes reveal a new mode of metallo-beta-lactamase inhibition. Chem Commun (Camb). 2017 May 4. doi: 10.1039/c7cc02394d. PMID:28470248 doi:http://dx.doi.org/10.1039/c7cc02394d
