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A structural link between inactivation and block of a K+ channel.

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A structural link between inactivation and block of a K+ channel. / Ader, Christian; Schneider, Robert; Hornig, Sönke; Velisetty, Phanindra; Wilson, Erica M; Lange, Adam; Giller, Karin; Ohmert, Iris; Martin-Eauclaire, Marie-France; Trauner, Dirk; Becker, Stefan; Pongs, Olaf; Baldus, Marc.

In: NAT STRUCT MOL BIOL, Vol. 15, No. 6, 6, 2008, p. 605-612.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Ader, C, Schneider, R, Hornig, S, Velisetty, P, Wilson, EM, Lange, A, Giller, K, Ohmert, I, Martin-Eauclaire, M-F, Trauner, D, Becker, S, Pongs, O & Baldus, M 2008, 'A structural link between inactivation and block of a K+ channel.', NAT STRUCT MOL BIOL, vol. 15, no. 6, 6, pp. 605-612. <http://www.ncbi.nlm.nih.gov/pubmed/18488040?dopt=Citation>

APA

Ader, C., Schneider, R., Hornig, S., Velisetty, P., Wilson, E. M., Lange, A., Giller, K., Ohmert, I., Martin-Eauclaire, M-F., Trauner, D., Becker, S., Pongs, O., & Baldus, M. (2008). A structural link between inactivation and block of a K+ channel. NAT STRUCT MOL BIOL, 15(6), 605-612. [6]. http://www.ncbi.nlm.nih.gov/pubmed/18488040?dopt=Citation

Vancouver

Ader C, Schneider R, Hornig S, Velisetty P, Wilson EM, Lange A et al. A structural link between inactivation and block of a K+ channel. NAT STRUCT MOL BIOL. 2008;15(6):605-612. 6.

Bibtex

@article{ab8198b478364966843cb87b4ab3634a,
title = "A structural link between inactivation and block of a K+ channel.",
abstract = "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.",
author = "Christian Ader and Robert Schneider and S{\"o}nke Hornig and Phanindra Velisetty and Wilson, {Erica M} and Adam Lange and Karin Giller and Iris Ohmert and Marie-France Martin-Eauclaire and Dirk Trauner and Stefan Becker and Olaf Pongs and Marc Baldus",
year = "2008",
language = "Deutsch",
volume = "15",
pages = "605--612",
journal = "NAT STRUCT MOL BIOL",
issn = "1545-9993",
publisher = "NATURE PUBLISHING GROUP",
number = "6",

}

RIS

TY - JOUR

T1 - A structural link between inactivation and block of a K+ channel.

AU - Ader, Christian

AU - Schneider, Robert

AU - Hornig, Sönke

AU - Velisetty, Phanindra

AU - Wilson, Erica M

AU - Lange, Adam

AU - Giller, Karin

AU - Ohmert, Iris

AU - Martin-Eauclaire, Marie-France

AU - Trauner, Dirk

AU - Becker, Stefan

AU - Pongs, Olaf

AU - Baldus, Marc

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

M3 - SCORING: Zeitschriftenaufsatz

VL - 15

SP - 605

EP - 612

JO - NAT STRUCT MOL BIOL

JF - NAT STRUCT MOL BIOL

SN - 1545-9993

IS - 6

M1 - 6

ER -