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Side-by-side comparison of Notch- and C83 binding to γ-secretase in a complete membrane model at physiological temperature
2022
γ-Secretase cleaves the C99 fragment of the amyloid precursor protein, leading to formation of aggregated β-amyloid peptide central to Alzheimer's disease, and Notch, essential for cell regulation. Recent cryogenic electron microscopy (cryo-EM) structures indicate major changes upon substrate binding, a β-sheet recognition motif, and a possible helix unwinding to expose peptide bonds towards nucleophilic attack. Here we report side-by-side comparison of the 303 K dynamics of the two proteins in
doi:10.17863/cam.85250
fatcat:fcxm5ajr4ngr5oirqhzrmqlm4m