Wednesday, September 20, 2006, 4:00 pm — Berkner Hall Auditorium
Proteins that cleave other proteins using a molecule of water, protease complexes are exquisite macromolecular machines involved in a multitude of physiological and cellular reactions. We have been studying two recently identified protease complexes using electron cryo-microscopy and X-ray crystallography. The first is a proteasome that resides in the cytoplasm of the Mycobacterial tuberculosis and is required for Tb resistance to destruction by human macrophages. The second is a gamma-secretase complex embedded in the cellular membrane of human neurons. Gamma-secretase produces Alzheimerï¿½s disease-causing A-beta peptides. Our structural studies shed light into the inner workings of these multi-protein assemblies, and they reveal a surprisingly common strategy for controlled proteolysis employed by the two drastically different machines. Further research will facilitate rational design of drugs for treating Tb infection and Alzheimerï¿½s disease.
Hosted by: Fulvia Pilat and Brant Johnson
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