Nucleophilic proteases: structure, function, regulation and disease

June 20–21, 2025
Virtual

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There are more than 600 proteases in the human genome making it the second largest family of proteins in humans. These proteolytic enzymes are tightly regulated and function by performing post-translational protein modifications through hydrolysis of peptide bonds which results in activation or deactivation of biological pathways in an enormous array of physiological processes. Dysregulated proteolysis is also implicated in a large, diverse set of diseases including those relating to cardiovascular, immunological and cancer. Furthermore, the pathogenesis of many infectious diseases is mediated by proteases, either from the microbe, the host or both.

These enzymes are classified by their catalytic mechanism into five types: serine, threonine, cysteine, aspartic and metalloproteases. This year we expand upon past meetings by highlighting the most significant recent studies not only on serine, but also on the other classes of nucleophilic threonine and cysteine proteases. The talks organized present aspects of protease biochemistry and biophysics such as structural biology, as well as drug discovery and inhibitor development. Cross-disciplinary topics include cancer, infectious disease (viruses, bacteria, other pathogens), inflammation and immunology, cardiovascular system, and others.

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