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. Author manuscript; available in PMC: 2021 Feb 1.
Published in final edited form as: Prog Neurobiol. 2019 Dec 18;185:101729. doi: 10.1016/j.pneurobio.2019.101729

Figure 1. Structural domain map of α-synuclein.

Figure 1.

Schematic representation of α-synuclein structural domains indicating the potential residues involved in nuclear and mitochondrial localization. Residues 1-60 and 103-140 are involved in the nuclear localization of α-synuclein (Ma et al., 2014). Residues 1-33 potentially contain a cryptic mitochondrial targeting signal (Devi et al., 2008). Missense α-synuclein mutations, including A30P, which is associated with familial PD, occur in the N-terminal domain. The aggregation-prone non-amyloidogenic region (NAC) is part of the membrane-binding domain. The C-terminal domain is proposed to be disordered and modulates interactions with various molecules including pro-oxidant metals associated with PD pathology.