R294H-D352H forms a lower affinity Zn site but is still able to promote the activated conformational state

(A and B) Normalized relationships from oocytes expressing (A) Kv1.2-R294H-D352H ( = 7) and (B) Kv1.2-D352H ( = 7) channels recorded in the absence (solid squares) and presence (open circles) of 1 μM Zn. (C) A plot of ΔV versus Zn concentration in oocytes expressing Kv1.2-R294H-D352H 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 470 nM ( = 5–10).

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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.