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. 2021 Sep;9(18):1397. doi: 10.21037/atm-21-1885

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2021 Annals of Translational Medicine. All rights reserved.

Open Access Statement: This is an Open Access article distributed in accordance with the Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International License (CC BY-NC-ND 4.0), which permits the non-commercial replication and distribution of the article with the strict proviso that no changes or edits are made and the original work is properly cited (including links to both the formal publication through the relevant DOI and the license). See: https://creativecommons.org/licenses/by-nc-nd/4.0.

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Structural analysis of Kv3.1 potassium channel involved known variants for MEAK, DEE, DE and myoclonus phenotypes. (A-C) The close view of different variants at positions of p.Arg317Ser, p.Arg320His and p.Arg421Val showed minimal disturbance for the adjacent configuration. (D-F) The close view of different variants at positions of p.Arg317His, p.Cys208Tyr and p.Thr399Met showed large steric hinderance, which likely disturb the protein structure or stability.