Human lactate dehydrogenase-A (LDHA) is emerging as a promising anticancer target. Up to now, structure-based investigations for identifying inhibitors of this enzyme have not explicitly accounted for active site flexibility. In the present study, by combining replica exchange molecular dynamics with network and cluster analyses, we identified reliable LDHA conformations for structure-based ligand design. The selected conformations were challenged and validated by retrospective virtual screening simulations.
R. Buonfiglio, M. Ferraro, F. Falchi, A. Cavalli, M. Masetti, M. Recanatini (2013). Collecting and assessing human lactate dehydrogenase-A conformations for structure-based virtual screening. JOURNAL OF CHEMICAL INFORMATION AND MODELING, 53, 2792-2797 [10.1021/ci400543y].
Collecting and assessing human lactate dehydrogenase-A conformations for structure-based virtual screening
BUONFIGLIO, ROSA;F. Falchi;CAVALLI, ANDREA;MASETTI, MATTEO;RECANATINI, MAURIZIO
2013
Abstract
Human lactate dehydrogenase-A (LDHA) is emerging as a promising anticancer target. Up to now, structure-based investigations for identifying inhibitors of this enzyme have not explicitly accounted for active site flexibility. In the present study, by combining replica exchange molecular dynamics with network and cluster analyses, we identified reliable LDHA conformations for structure-based ligand design. The selected conformations were challenged and validated by retrospective virtual screening simulations.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
