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. 2015 Aug 28;47(8):e179. doi: 10.1038/emm.2015.54

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Copyright © 2015 KSBMB.

This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by-nc-nd/4.0/

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Structure of full length α-SYN protein and its functional components. N-terminal (1–60), non-Aβ component of amyloid plaques domain (61–95) and C-terminal (96–140); point mutations reported in familial PD (autosomal dominant form) are present in the N-terminal (red arrows). N-terminal contributes to the α-helical structure of α-SYN upon binding to lipid membranes. Non-Aβ component of amyloid plaques domain contains most hydrophobic residues and one phosphorylation site (blue rectangle, serine 87). Non-Aβ component of amyloid plaques domain promotes aggregation of the molecule by its propensity to form β-sheet structure. C-terminal has three nitration sites (green circle, tyrosine 125, 133, 136) and one phosphorylation site (blue rectangle, serine S129) and is mainly responsible for maintaining the protein solubility.