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Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions

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Department of Chemistry, Center for Research and Advanced Studies (Cinvestav), 07360 Mexico City, Mexico
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Institute of Neuroscience and Medicine (INM-9) and Institute for Advanced Simulation (IAS-5), Forschungszentrum Jülich, Wilhelm-Johnen-Strasse, 52425 Jülich, Germany
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Jülich Supercomputing Center (JSC), Forschungszentrum Jülich, 52428 Jülich, Germany
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Department of Oncology, Hematology and Stem Cell Transplantation, Faculty of Medicine, RWTH Aachen University, Pauwelsstraße 30, 52074 Aachen, Germany
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Department of Physics and Department of Neurobiology, RWTH Aachen University, 52078 Aachen, Germany
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Institute for Neuroscience and Medicine (INM)-11, Forschungszentrum Jülich, 52428 Jülich, Germany
*
Authors to whom correspondence should be addressed.
Current Address: Instituto de Biología Molecular y Celular de Rosario (IBR-CONICET), Ocampo y Esmeralda, 2000 Rosario, Argentina.
Int. J. Mol. Sci. 2019, 20(1), 18; https://doi.org/10.3390/ijms20010018
Received: 3 December 2018 / Revised: 17 December 2018 / Accepted: 18 December 2018 / Published: 20 December 2018
The N-terminus of the prion protein is a large intrinsically disordered region encompassing approximately 125 amino acids. In this paper, we review its structural and functional properties, with a particular emphasis on its binding to copper ions. The latter is exploited by the region’s conformational flexibility to yield a variety of biological functions. Disease-linked mutations and proteolytic processing of the protein can impact its copper-binding properties, with important structural and functional implications, both in health and disease progression. View Full-Text
Keywords: N-terminal prion protein; copper binding; prion disease mutations N-terminal prion protein; copper binding; prion disease mutations
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Sánchez-López, C.; Rossetti, G.; Quintanar, L.; Carloni, P. Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions. Int. J. Mol. Sci. 2019, 20, 18.

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