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Paetzel Lab
Protease Structure-Function and Inhibitor Design.
Welcome!
We determine the 3D-structure of viral and bacterial proteolytic enzymes.
These enzymes catalyze essential cleavage steps within proteins and peptides that are important for infection and disease. The 3D structures help to reveal the catalytic mechanism of these enzymes. This in turn inspires the design of molecules that can inhibit the enzyme and thereby lead to antiviral and antibacterial compounds. We clone, express and purify the proteases and their substrates and investigate their mechanism through a combination of site-directed mutagenesis, chemical modifications and kinetics. We crystallize the proteases and determine their structure using X-ray crystallography. We are experts in trapping the acyl-enzyme complex of serine and cysteine proteases. We use a combination of computational and experimental methods to design and test protease inhibitors. We are always looking for motivated and team oriented students to help us with this work.
For more details, visit our research lab website.
Selected Publications
- Lee, J. et al. X-ray crystallographic characterization of the SARS-CoV-2 main protease polyprotein cleavage sites essential for viral processing and maturation. Nature Communications 2022
- Lee et al. Crystallographic structure of wild-type SARS-CoV-2 main protease acyl-enzyme intermediate with physiological C-terminal autoprocessing site. Nature Communications 2020
- Paetzel, M. Bacterial Signal Peptidases. Subcellular Biochemistry 2019
- View more publications