Skip to main content
. Author manuscript; available in PMC: 2024 Feb 1.
Published in final edited form as: Trends Neurosci. 2022 Dec 23;46(2):153–166. doi: 10.1016/j.tins.2022.11.007

Figure 1. α-Synuclein domain structure.

Figure 1.

(A, B) α-Synuclein is composed of an N-terminal membrane binding region that mediates its association with synaptic vesicles through formation of an amphipathic α-helix, and a C-terminal region that binds to VAMP2 (A). The N-terminal region can be further divided into eleven imperfect KTKEGV repeats (B), and contains the aggregation-prone NAC domain. Several mutations in α-synuclein have been identified that lead to disease (purple) or with yet unknown significance (pink). (C, D) Analysis of the position of mutations within the repetitive KTKEGV regions highlights that mutations cluster in repeat position 5, 10 and 11, while other positions are spared (C). Clusters at positions 10 and 11 face towards the membrane, while cluster 5 faces towards the cytosol (D).