Coupling of activation and inactivation gate in a K+-channel: potassium and ligand sensitivity.
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Coupling of activation and inactivation gate in a K+-channel: potassium and ligand sensitivity. / Ader, Christian; Schneider, Robert; Hornig, Sönke; Velisetty, Phanindra; Vardanyan, Vitya; Giller, Karin; Ohmert, Iris; Becker, Stefan; Pongs, Olaf; Baldus, Marc.
in: EMBO J, Jahrgang 28, Nr. 18, 18, 2009, S. 2825-2834.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Coupling of activation and inactivation gate in a K+-channel: potassium and ligand sensitivity.
AU - Ader, Christian
AU - Schneider, Robert
AU - Hornig, Sönke
AU - Velisetty, Phanindra
AU - Vardanyan, Vitya
AU - Giller, Karin
AU - Ohmert, Iris
AU - Becker, Stefan
AU - Pongs, Olaf
AU - Baldus, Marc
PY - 2009
Y1 - 2009
N2 - Potassium (K(+))-channel gating is choreographed by a complex interplay between external stimuli, K(+) concentration and lipidic environment. We combined solid-state NMR and electrophysiological experiments on a chimeric KcsA-Kv1.3 channel to delineate K(+), pH and blocker effects on channel structure and function in a membrane setting. Our data show that pH-induced activation is correlated with protonation of glutamate residues at or near the activation gate. Moreover, K(+) and channel blockers distinctly affect the open probability of both the inactivation gate comprising the selectivity filter of the channel and the activation gate. The results indicate that the two gates are coupled and that effects of the permeant K(+) ion on the inactivation gate modulate activation-gate opening. Our data suggest a mechanism for controlling coordinated and sequential opening and closing of activation and inactivation gates in the K(+)-channel pore.
AB - Potassium (K(+))-channel gating is choreographed by a complex interplay between external stimuli, K(+) concentration and lipidic environment. We combined solid-state NMR and electrophysiological experiments on a chimeric KcsA-Kv1.3 channel to delineate K(+), pH and blocker effects on channel structure and function in a membrane setting. Our data show that pH-induced activation is correlated with protonation of glutamate residues at or near the activation gate. Moreover, K(+) and channel blockers distinctly affect the open probability of both the inactivation gate comprising the selectivity filter of the channel and the activation gate. The results indicate that the two gates are coupled and that effects of the permeant K(+) ion on the inactivation gate modulate activation-gate opening. Our data suggest a mechanism for controlling coordinated and sequential opening and closing of activation and inactivation gates in the K(+)-channel pore.
M3 - SCORING: Zeitschriftenaufsatz
VL - 28
SP - 2825
EP - 2834
JO - EMBO J
JF - EMBO J
SN - 0261-4189
IS - 18
M1 - 18
ER -