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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 4. Comparative analysis of two DNA-protein docking methods for three characterized PDB structures of α-synuclein.

Figure 4.

Amino acid residues 60-100 within the NAC domain are the most likely to interact with DNA when α-synuclein adopts an α-helical folded conformation (PDB ID: 1XQ8 and 2KKW). Amino acids residues located in either the N-terminal or the C-terminal of the α-synuclein fibril structure (PDB ID: 2N0A) are more free to interact with DNA.