Structural studies of 14-3-3 protein complexes and their stabilization by small molecule compounds (PhD student presentation)
by M.Sc., Domenico Lentini Santo
Protein-protein interactions (PPIs) play a crucial role in almost all biological processes. Many proteins require a number of dynamic interactions with other proteins and/or biomolecules to function. A detailed insight into PPIs is essential for a complete understanding of the processes mediated by these protein complexes. Because many PPIs are involved in disease-related signaling pathways, such PPIs are important targets for pharmaceutical interventions, especially in situations where a more conventional target (e.g. the active site of an enzyme, the binding site of a receptor) cannot be used. My doctoral project focused on 14-3-3 proteins, a family of eukaryotic adaptor and scaffolding proteins involved in the regulation of many signaling pathways. The main aim was to structurally characterize 14-3-3 protein complexes with selected binding
partners and investigate their stabilization by small molecule compounds.
Organizers: Prof. Tomáš Obšil, Prof. Jiří Čejka, Dr. Jan Přech
