Molecular glues stabilizing 14-3-3 Protein-Protein Interactions: a QBI Online Seminar with Christian Ottmann

The QBI Seminar Series is presenting Christian Ottmann, an Associate Professor of Molecular Cell and Structural Biology in the Department of Biomedical Engineering at the Eindhoven University of Technology. Dr. Ottmann works on small-molecule modulation of 14-3-3 Protein-Protein Interactions with a special focus on natural products and their derivatives. He was coordinator of the FP7 Industry-Academia Partnership and Pathways 14-3-3STABS and the Horizon2020 European Training Network TASPPI. Before taking up his current position in Eindhoven, Dr. Ottmann was a group leader at the Chemical Genomics Centre of the Max Planck Society in Dortmund, Germany. He obtained his Ph.D. in 2003 from the University of Tübingen with Prof. Claudia Oecking. Since July 2020 he works as co-funder and CTO at Ambagon Therapeutics.

14-3-3 is probably the most widely connected hub protein in human biology, interacting with hundreds of partner proteins. Many of these clients play important roles in disease, for example p53 (cancer), LRRK2 (Parkinson’s), Tau (Alzheimer’s) and CFTR (cystic fibrosis). Binding to 14-3-3 modulates the disease-related activity of these proteins and small-molecule stabilization of the respective 14-3-3 complexes could convey a therapeutic benefit. In his talk, Dr. Ottmann will show some examples of how he and his team identified and characterized compounds that stabilize 14-3-3 protein-protein interactions. His talk will focus on the crystallographic and biophysical analysis of the three-body system encompassing 14-3-3, the partner protein and the molecular glue.

Talk title: Molecular glues stabilizing 14-3-3 Protein-Protein Interactions

Hosted by: Michelle Arkin