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Interaction between the Prion Protein’s Copper-Bound Octarepeat Domain and a Charged C-terminal Pocket Suggests a Mechanism for N-terminal Regulation

Copper plays a critical role in prion protein (PrP) physiology. Cu(2+) binds with high affinity to the PrP N-terminal octarepeat domain (OR), and intracellular copper promotes PrP expression. The molecular details of copper coordination within the OR are now well characterized. Here we examine how C...

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Detalles Bibliográficos
Publicado en:Structure
Main Authors: Evans, Eric G. B., Pushie, M. Jake, Markham, Kate A., Lee, Hsiau-Wei, Millhauser, Glenn L.
Formato: Artigo
Idioma:Inglês
Publicado: 2016
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Acceso en liña:https://ncbi.nlm.nih.gov/pmc/articles/PMC4938727/
https://ncbi.nlm.nih.gov/pubmed/27265848
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1016/j.str.2016.04.017
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