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A structural link between inactivation and block of a K+ channel
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Journal Article
A structural link between inactivation and block of a K+ channel
2008
Overview
Gating the ion-permeation pathway in K
+
channels requires conformational changes in activation and inactivation gates. Here we have investigated the structural alterations associated with pH-dependent inactivation gating of the KcsA-Kv1.3 K
+
channel using solid-state NMR spectroscopy in direct reference to electrophysiological and pharmacological experiments. Transition of the KcsA-Kv1.3 K
+
channel from a closed state at pH 7.5 to an inactivated state at pH 4.0 revealed distinct structural changes within the pore, correlated with activation-gate opening and inactivation-gate closing. In the inactivated K
+
channel, the selectivity filter adopts a nonconductive structure that was also induced by binding of a pore-blocking tetraphenylporphyrin derivative. The results establish a structural link between inactivation and block of a K
+
channel in a membrane setting.
Publisher
Nature Publishing Group US,Nature Publishing Group
Subject
/ Biochemistry, Molecular Biology
/ Biomedical and Life Sciences
/ Ions
/ Kv1.3 Potassium Channel - chemistry
/ Kv1.3 Potassium Channel - physiology
/ Magnetic Resonance Spectroscopy
/ Micelles
/ NMR
/ Potassium Channels, Voltage-Gated
/ Potassium Channels, Voltage-Gated - chemistry
