ATOMIC STRUCTURE OF A PRP-FC FUSION PROTEIN

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. A modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPc form, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. Using recombinant prion proteins, the C terminus of PrPc has been solved by NMR and x-ray crystallography, but the N terminus was found to be unstructured. In this proposal, we will employ an eukaryotically expressed fusion protein, PrP-Fc, to solve the complete structure of PrPc through x-ray crystallography.