Institute of Structural Biology
University of Bonn
Welcome to our Institute! We are interested in the structure–function relationship of biological macromolecules. We use molecular biology techniques, biochemistry, biophysics, X-ray crystallography and cryo electron microscopy to investigate biological phenomena at atomic resolution.
![New paper in Cell Chemical Biology](/images/jan_gerhartz_mugshot_300px.jpg)
New paper in Cell Chemical Biology
Congratulations to Jan Gerhartz for his first publication of a PhD in the Nowak Lab! Jan wrote a perspective article summarizing a new concept of bifunctional small molecules that can dimerize proteins and therefore generate a more potent and selective inhibitors. Small molecule inhibition relies on maintaining high occupancy of the protein target and are frequently limited for potency and selectivity. These types of inhibitors have been recently developed to target an E3 ubiquitin ligase KEAP1. KEAP1, controlled by the redox activity of the cell is known to degrade transcription factor Nrf2. Nrf2 is known for its importance in acute inflammat...
![New paper in Nature Communications](/images/Anja_small_news.jpg)
New paper in Nature Communications
A new way to inhibit pyroptosis! Anja characterized by biochemical means six nanobodies that were raised against human Gasdermin D. All of them bind to the N-terminal domain of this membrane rupturing protein, but three specifically block the assembly of the membrane pore. She succeeded in crystallizing full length Gasdermin D together with two nanobodies and determined the structure at 1.9 Å resolution, providing first structural insights into the mode of action of nanobody-based Gasdermin D inhibition. Read the full story here....
![New paper in JBC](/images/Max_kicker_website.jpg)
New paper in JBC
SR-4835, a small molecule inhibitor currently in phase I clinical trials, targets transcriptional kinases Cdk12 and Cdk13. Biochemical and structural analyses could highlight SR-4835’s selectivity towards Cdk12/Cdk13 over other CMGC kinase family members. We determined the crystal structure of the Cdk12/CycK heterodimer in complex with SR-4835 at 2.7Å resolution, revealing a unique hydrogen bond network mediated by the kinase hinge region. The structural insights provided offer a foundation for optimization and design of reversible Cdk12-specific inhibitors and could facilitate the basis for the development of novel cancer therapeutics. The fu...
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