Metal ion binding to R294H-A351H stabilizes the activated state after neutralization of acidic residues D352 and E353

(A) Representative current traces from an oocyte expressing Kv1.2-R294H-A351H-D352G-E353S channels recorded in the absence (left) and presence (right) of 1 μM Zn, using the protocol outlined in the Materials and methods. (B) Normalized relationships from oocytes expressing Kv1.2-R294H-A351H-D352G-E353S channels recorded in the absence (solid squares, 9) and presence (open circles, 9) of 1 μM Zn. (C) A plot of ΔV versus Zn concentration in oocytes expressing Kv1.2-R294H-A351H-D352G-E353S channels, where ΔV is the difference between the fitted V values obtained in the absence and presence of varying concentrations of Zn. The data were fitted with a hyperbolic function (solid curve) with a half-maximal concentration of 0.36 ± 0.18 μM ( = 4–8). (D and E) Normalized curves obtained in the absence (solid squares) and presence (open circles) of 1 μM Zn for (D) Kv1.2-R294H-D352G-E353S ( = 7) and (E) Kv1.2-A351H-D352G-E353S ( = 7).

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Taken from "Atomic Constraints between the Voltage Sensor and the Pore Domain in a Voltage-gated K Channel of Known Structure"

The Journal of General Physiology 2008;131(6):549-561.

Published online Jan 2008

PMCID:PMC2391244.