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  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., Zweckstetter, M., Carloni, P., Selenko, P., et al. (2015). Copper binding to the N-terminally acetylated, naturally occurring form of alpha-synuclein induces local helical folding. Journal of the American Chemical Society, 137(20), 6444-6447. doi:10.1021/jacs.5b01911.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-7D83-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002A-5179-D
Genre: Journal Article

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 Creators:
Miotto, M. C., Author
Valiente-Gabioud, A. A., Author
Rossetti, G., Author
Zweckstetter, M.1, Author              
Carloni, P., Author
Selenko, P., Author
Griesinger, C.2, Author              
Binolfi, A., Author
Fernández, C. O., Author
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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 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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Language(s): eng - English
 Dates: 2015-05-042015
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1021/jacs.5b01911
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Title: Journal of the American Chemical Society
Source Genre: Journal
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Pages: - Volume / Issue: 137 (20) Sequence Number: - Start / End Page: 6444 - 6447 Identifier: -