ProteoCure Webinar

Hans Brandstetter

Thursday, April 04th 2024, at 13.00 CET

The CD clan cysteine proteases: Unique structures, unique mechanisms and unique functions

Hans Brandstetter received a Ph.D. in chemistry summa cum laude from the Technical University of Munich in 1994. He conducted postdoctoral research at the Massachusetts Institute of Technology and Harvard Medical School, Cambridge/Boston, and Max-Planck-Institute, Martinsried. In 2003 he was appointed Chief Scientific Officer at proteros GmbH, Martinsried/Munich. Dr. Brandstetter was recruited to the University of Salzburg in 2005.

Webinar Summary: Clan CD cysteine proteases such as caspases, legumain and separase share a unique arrangement of their catalytic cysteine-histidine dyad. This non-canonical dyad structure explains unique reactivities in this protease clan, including their critical dependence on the pH. Here, I illustrate the activity regulation principles derived for legumain and discuss how these principles can be applied to understand the puzzling activation of other members of the CD clan, including metacaspases and the paracaspase MALT1.

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