6. Protein Interactions, Conversion Intermediates, and Oligomers of PrP
Principal Investigator: Julie Forman-Kay, Hospital for Sick Children
Co-Investigators:
Avijit Chakrabartty, University of Toronto
Lewis Kay, University of Toronto
Simon Sharpe, University of Toronto
Collaborators:
Joaquin Castilla, Scripps Research Institute
Valerie Sim, University of Alberta
Gerald Schmitt-Ulms, University of Toronto
Brian Shilton, University of Western Ontario
Frank Sonnichsen, Case Western Reserve University
Witold Surewicz, Case Western Reserve University
David Westaway, University of Alberta
David Wishart, University of Alberta
Shoshana Wodak, Hospital for Sick Children
Project Description:
The prion protein (PrP) is the major causative agent of neurodegenerative prion diseases. PrP is capable of changing protein conformation from the normal to the infectious form. The altered structure interacts with other proteins that may cause toxicity in prion diseases. Using nuclear magnetic resonance (NMR) spectroscopy, the team is studying the various intermediate structures that occur as the PrP converts or “misfolds” into its infectious form and wil also investigate how they interact with other proteins. Results will provide information about the mechanism of infection, toxicity, the normal function of PrP, and ultimately contribute to developing treatments for prion diseases.
(Open Call II)
Last Updated: 4/16/2010 8:26:18 PM
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