Correcting congenital myasthenia-associated acetylcholine receptor defects - Nature

Data availabilityAll atomic models and cryo-EM maps have been deposited in the Protein Data Bank and Electron Microscopy Data Bank: εP121L + ACh (PDB 9YE6, EMD-72844); εP121L + ACh, +XG-590 (PDB 9YE7, EMD-72845); εL269F + ACh (PDB 9YE8, EMD-72846); εL269F + ACh, +Reboxetine, upper pore (PDB 9YEH, EMD-72850); εL269F + ACh, +Reboxetine, lower pore 1 (PDB 9YEI, EMD-72851); εL269F + ACh, +Reboxetine, lower pore 2 (PDB 9YEK, EMD-72853); εL269F + ACh, +Fluoxetine (PDB 9YEL, EMD-72854); εT264P + ACh (PDB 9YER, EMD-72860); εT264P + ACh, +Reboxetine (PDB 9YET, EMD-72862); βV266M + ACh (PDB 9YEU, EMD-72863); βV266M + ACh, +Quinidine (PDB 9YEX, EMD-72866); αV249F + ACh, +Fluoxetine (PDB 9YF0, EMD-72868). The wild-type muscle receptor in apo (PDB 9DMG) and ACh-bound (PDB 9DMH) states were used to perform structural analyses. All other materials are available upon request.ReferencesEngel, A. G., Shen, X.-M., Selcen, D. & Sine, S. M. Congenital myasthenic syndromes: pathogenesis, diagnosis, and treatment. Lancet Neurol. 14, 420–434 (2015).Article

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Li, H., Teng, J. & Hibbs, R. E. Structural switch in acetylcholine receptors in developing muscle. Nature 632, 1174–1180 (2024).Article