Journal Article

FZJ-2015-05061

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Copper Binding to the N-Terminally Acetylated, Naturally Occurring Form of Alpha-Synuclein Induces Local Helical Folding

Miotto, M. C. ; Valiente-Gabioud, A. A. ; Rossetti, G.FZJ* ; Zweckstetter, M. ; Carloni, P.FZJ* ; Selenko, P. ; Griesinger, C. ; Binolfi, A. (Corresponding author) ; Fernández, C. O. (Corresponding author)

2015
American Chemical Society Washington, DC

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Please use a persistent id in citations: doi:10.1021/jacs.5b01911

Abstract: Growing evidence supports a link between brain copper homeostasis, the formation of alpha-synuclein (AS)-copper complexes, and the development of Parkinson disease (PD). Recently it was demonstrated that the physiological form of AS is N-terminally acetylated (AcAS). Here we used NMR spectroscopy to structurally characterize the interaction between Cu(I) and AcAS. We found that the formation of an AcAS–Cu(I) complex at the N-terminal region stabilizes local conformations with α-helical secondary structure and restricted motility. Our work provides new evidence into the metallo-biology of PD and opens new lines of research as the formation of AcAS–Cu(I) complex might impact on AcAS membrane binding and aggregation.

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Contributing Institute(s):

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

Research Program(s):

1. 511 - Computational Science and Mathematical Methods (POF3-511) (POF3-511)

Appears in the scientific report 2015

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Database coverage:
; BIOSIS Previews ; Current Contents - Life Sciences ; Current Contents - Physical, Chemical and Earth Sciences ; IF >= 10 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Thomson Reuters Master Journal List ; Web of Science Core Collection

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