
The cover picture shows the binding of a PLHSpT derivative, 6q, to the polo-like kinase 1 (Plk1) polo-box domain (PBD), thereby uncovering a new hydrophobic channel (magnified upper right), which is absent in the unliganded protein (magnified lower left). The authors explain how, as a consequence of the additional interaction with the channel, the peptide binds to the Plk1 PBD with a binding affinity more than two orders of magnitude higher. The background image of a stained cell nucleus depicts how this binding results in interference with Plk1 (red dots)-dependent bipolar spindle formation (green), and this ultimately leads to mitotic block and apoptotic cell death in cultured cancer cells.
Fa Liu, Jung-Eun Park, Wen-Jian Qian, Dan Lim, Andrej Scharow, Thorsten Berg, Michael B. Yaffe, Kyung S. Lee*, and Terrence R. Burke Jr., in ChemBioChem , 2012, 13, 1291-1296.