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. Author manuscript; available in PMC: 2019 Oct 24.
Published in final edited form as: Biochim Biophys Acta Biomembr. 2018 Apr 24;1860(9):1698–1708. doi: 10.1016/j.bbamem.2018.04.002

Figure 1.

Figure 1

Yellow shading represents hydrophobic core of the membrane. Red residues contain familial AD mutations. Blue residues are critical to the formation of C99 dimers. Green residues may be phosphorylated. Purple residues form the lysine anchor. Black residues indicate γ-secretase cleavage sites and metal binding residues. Brown residues are critical for C31 formation and cytotoxicity. Cylinders represent domains with significant helical propensity. θ and κ angles describe the TMD tilt and GG hinge angle. The θ angle increases with thinning or curving of the membrane surface, and κ increases with curving of the membrane surface. Black solid lines mark the membrane surface and black dashed lines represent the membrane hydrophobic core. The orange lipid marks the putative cholesterol binding site. Also shown is an atomistic structure of C99 predicted from TALOS+ using LMPG micelle backbone chemical shifts and secondary structure assigned with STRIDE. Cα within the atomistic structure are labeled as N-terminal familial AD mutation (red), residues 28, 37, 38, 53,54, and 55 (orange), phosphorylatable residues Cα (green), and C-Helix (blue).