Skip to main content
. 2018 Aug 7;9:3126. doi: 10.1038/s41467-018-05616-4

Fig. 6.

Fig. 6

The influence of a patient-specific mutation on ATP-dependent activation. a Representative current traces recorded from hBest1 I201T iPSC-RPE in the absence or presence of 2 mM ATP (Scale bar, 300 pA, 100 ms). b Population steady-state current–voltage relationships in hBest1 I201T iPSC-RPE in the absence or presence of 2 mM ATP; n = 5–6 for each point. c The MST binding curves of KpBest L177T (red) to ATPγS. Protein fraction bound vs. [ATPγS], n = 3 for each point. The binding curve of WT KpBest to ATPγS (black) is shown for comparison. d Representative current trace of single KpBest L177T mutant channel recorded from planar lipid bilayers at 80 mV in the presence of 2 mM ATP (Scale bar, 2 pA, 250 ms). e Bar chart showing the open probability of KpBest WT and L177T channels in the presence of 2 mM ATP, n = 3 for each bar. *P < 0.05 compared to the open probability of WT KpBest in the presence of ATP, using two-tailed unpaired Student t test. All error bars in this figure represent s.e.m.