Figure 4

V407F interacts with M411. (a) Local conformational changes in the IDF of the V407F mutant crystal structure (salmon) compared to that of the WT structure (grey). (b) In MD simulations, the distance distribution histogram shows a shorter distance between residue 407 and residue 411 in the V407F mutant protein complex compared to the WT complex. (c) M411A mutation right-shifted the Ca²⁺ dependent activation of the V407F mutant SK2-a channel. (d) M411A mutation significantly compromised the Ca²⁺ hypersensitivity of the V407F mutant SK2-a channel. Statistical analysis was performed using one-way ANOVA followed by Tukey’s post hoc tests. All data are presented in mean ± s.e.m.