Journal Article

FZJ-2018-07587

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Structural Determinants of the Prion Protein N-Terminus and Its Adducts with Copper Ions

Sánchez-López, C. ; Rossetti, G.FZJ* ; Quintanar, L. (Corresponding author) ; Carloni, P. (Corresponding author)FZJ*

2019
Molecular Diversity Preservation International Basel

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Please use a persistent id in citations: http://hdl.handle.net/2128/21125  doi:10.3390/ijms20010018

Abstract: 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.

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Contributing Institute(s):

1. Computational Biomedicine (IAS-5)
2. Jülich Supercomputing Center (JSC)
3. Computational Biomedicine (INM-9)

Research Program(s):

1. 571 - Connectivity and Activity (POF3-571) (POF3-571)
2. 574 - Theory, modelling and simulation (POF3-574) (POF3-574)
3. 511 - Computational Science and Mathematical Methods (POF3-511) (POF3-511)

Appears in the scientific report 2019

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Database coverage:
; ; ; ; Clarivate Analytics Master Journal List ; Current Contents - Physical, Chemical and Earth Sciences ; DOAJ Seal ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; PubMed Central ; SCOPUS ; Science Citation Index Expanded ; Web of Science Core Collection

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