Fig. 3: Structural analysis of gS87, pS87, unmodified WT, and pY39 α-syn fibril.
From: Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures
a The structural model of gS87 fibril, with the zoom-in views the interactions between GlcNAc, K80, E61, T81, V82, I88 and A89, and the hydrophobic zipper-like interactions with the involved residues labeled. b The structure of unmodified WT α-syn fibril, with the conformation of S87 and the salt bridge between K80 and E46 shown in the zoom-in views. c The structure of pS87 fibril, with the hydrophobic interactions of the interface between two protofilaments, and two pairs of salt bridges shown in the zoom-in views. Residues involved in the inter-protofilamental interactions are shown in spheres. d The structure of pY39 fibril with the electrostatic interactions of the phosphate group bound to Y39 and K21, K32 and K34 shown in the zoom-in view. Distances are shown in Å. The PDB code of each fibril structure is indicated.
