5n4s
VIM-2 metallo-beta-lactamase in complex with ((S)-3-mercapto-2-methylpropanoyl)-D-tryptophan (Compound 3)VIM-2 metallo-beta-lactamase in complex with ((S)-3-mercapto-2-methylpropanoyl)-D-tryptophan (Compound 3)
Structural highlights
FunctionPublication Abstract from PubMedCrystallographic 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. See AlsoReferences
|
|