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. Author manuscript; available in PMC: 2023 Jun 1.
Published in final edited form as: Curr Opin Struct Biol. 2022 Apr 20;74:102373. doi: 10.1016/j.sbi.2022.102373

Figure 4.

Figure 4.

(A) Computational model of γ-secretase that is embedded in a lipid bilayer and solvated in 0.15 M NaCl aqueous solution. (B) All-atom GaMD simulations captured spontaneous activation of γ-secretase, during which the enzyme active site was poised for proteolysis of the APP substrate at the ε cleavage site. (C) Active (wildtype) and (D) shifted active (M51F) conformational states of the APP substrate-bound γ-secretase. Distinct APP intracellular domain (AICD) products were generated from the wildtype and M51F mutant APP.