Figure 1.
Binding pocket and modulation mechanism of Bay k 8644 in Cav1.1 channel. (A) Close-up of the binding pocket of Cav1.1 with S Bay k 8644, taken from the cryo-EM structure (PDB: 7JPL) (Gao and Yan, 2021). (B) Depiction of the two enantiomers of Bay k 8644 and their preferred helical conformation in S6III and S6IV shown above. The authors found that the S enantiomer, the agonist, had more favorable interactions with the Cav channel when both the S6III and S6IV helices were π-helices. The R enantiomer, the antagonist, was found to have more favorable interactions when the S6III helix was a π-helix, and the S6IV an α-helix. (C) Molecular graph of Bay k 8644, with the chiral center indicated.

Binding pocket and modulation mechanism of Bay k 8644 in Cav1.1 channel. (A) Close-up of the binding pocket of Cav1.1 with S Bay k 8644, taken from the cryo-EM structure (PDB: 7JPL) (Gao and Yan, 2021). (B) Depiction of the two enantiomers of Bay k 8644 and their preferred helical conformation in S6III and S6IV shown above. The authors found that the S enantiomer, the agonist, had more favorable interactions with the Cav channel when both the S6III and S6IV helices were π-helices. The R enantiomer, the antagonist, was found to have more favorable interactions when the S6III helix was a π-helix, and the S6IV an α-helix. (C) Molecular graph of Bay k 8644, with the chiral center indicated.

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