title: Hitting a moving target: targeting transient protein states.
abstract: In this issue of Structure, Bista and colleagues report that inhibitors of the MDM2/p53 interaction can be designed to interact with a transiently folded α-helical segment of the MDM2 lid region. This suggests that targeting transient protein states in PPI inhibitor design could be a promising strategy to improve affinity and/or selectivity profiles.
authors: Laboratory for Molecular Design and Pharmaceutical Biophysics, Department of Pharmaceutical and Medicinal Chemistry, Institute of Pharmacy, Eberhard Karls University Tuebingen, Auf der Morgenstelle 8, 72076 Tuebingen, Germany.
authors: Matthias R
authors: MR
authors: Bauer
authors: Frank M
authors: FM
authors: Boeckler
mesh_terms: D004151:Dipeptides / Q000737:chemistry*; D006801:Humans; D006877:Hydroxamic Acids / Q000737:chemistry*; D051736:Proto-Oncogene Proteins c-mdm2 / Q000737:chemistry*; D014364:Tryptophan / Q000031:analogs & derivatives* / Q000737:chemistry; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry*
chemical_list: D004151:Dipeptides; D006877:Hydroxamic Acids; C000591451:KK271 compound; D016159:Tumor Suppressor Protein p53; C000591452:YH300 compound; D014364:Tryptophan; C497206:MDM2 protein, human; D051736:Proto-Oncogene Proteins c-mdm2