Figure 6.
Kinetic model of KV10.2 and its interaction with the S4-S5L peptide. A, kinetic model schemes. This model is based on a previous work on KCNE1-KCNQ1 (23). a, kinetic model in the absence of peptide, on which optimization has been performed (see “Experimental procedures”). Optimized transition rates are presented in Table 1. b, binding of exogenous S4-S5L locks the channel and prevents its opening. Peptides are supposed to interact with each monomer in the unlocked states. B, simulated currents during step protocols (same as in Fig. 5), in the absence (Ctrl) or presence of S4-S5L peptide, at the indicated S4-S5L on/off rates. C, gray filled circles: experimental activation curves and half-activation times in control condition. Other symbols: simulated values in the absence of peptide (control, open circles), or in the presence of peptides, at the indicated rates of peptide binding/unbinding.