Copper- and Zinc-Promoted Interdomain Structure in the Prion Protein: A Mechanism for Autoinhibition of the Neurotoxic N-Terminus.

Abstract

The function of the cellular prion protein (PrPC), while still poorly understood, is increasingly linked to its ability to bind physiological metal ions at the cell surface. PrPC binds divalent forms of both copper and zinc through its unstructured N-terminal domain, modulating interactions between PrPC and various receptors at the cell surface and… (More)
DOI: 10.1016/bs.pmbts.2017.06.005

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Cite this paper

@article{Evans2017CopperAZ, title={Copper- and Zinc-Promoted Interdomain Structure in the Prion Protein: A Mechanism for Autoinhibition of the Neurotoxic N-Terminus.}, author={Eric Evans and Glenn L. Millhauser}, journal={Progress in molecular biology and translational science}, year={2017}, volume={150}, pages={35-56} }