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Copper plays a critical role in prion protein (PrP) physiology. Cu2+ binds with high affinity to the PrP N-terminal octarepeat (OR) domain, and intracellular copper promotes PrP expression. The molecular details of copper coordination within the OR are now well characterized. Here we examine how Cu2+ influences the interaction between the PrP N-terminal domain and the C-terminal globular domain. Using...
The cellular prion protein PrP C consists of two domains—a flexible N-terminal domain, which participates in copper and zinc regulation, and a largely helical C-terminal domain that converts to β sheet in the course of prion disease. These two domains are thought to be fully independent and noninteracting. Compelling cellular and biophysical studies, however, suggest a higher order structure...