Elsevier, Structure, 12(21), p. 2095-2097, 2013
DOI: 10.1016/j.str.2013.11.003
Full text: Unavailable
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.