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

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

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作者：Eric G.B. Evans¹ ; M. Jake Pushie² ; Kate A. Markham¹ ; Hsiau-Wei Lee¹ ; Glenn L. Millhauser¹ ; ^{glennm@ucsc.edu" class="auth_mail" title="E-mail the corresponding author}
刊名：Structure
出版年：2016
出版时间：6 July 2016
年：2016
卷：24
期：7
页码：1057-1067
全文大小：2751 K

文摘

•: The N-terminal octarepeat domain of the prion protein takes up Cu²⁺
•: The octarepeat Cu²⁺ interacts with a negatively charged C-terminal domain pocket
•: The C-terminal interaction surface overlaps the epitope of the toxic POM1 antibody
•: POM1 may act by interfering with the Cu²⁺ promoted cis interaction

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