Abstract
The pathogenesis of prion diseases is initiated when the cellular prion protein (PrPC) is misfolded into the scrapie prion protein (PrPSc). PrPC is composed of two major domains, the N-terminal intrinsically disordered tail and the C-terminal globular domain. These domains interact with each other via a copper(II)-driven cis interaction. The proposed model of this tertiary structure is a Cu2+ ion coordinated to three histidines in the N-terminal tail and one histidine in the C-terminal domain. To test this hypothesis, the N-terminal tail of PrPC is segmentally 15N-isoptically labeled via transpeptidation by 7M sortase A enzyme.
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