A molecular switch driving inactivation in the cardiac K+ channel HERG.

Autor: David A Köpfer, Ulrike Hahn, Iris Ohmert, Gert Vriend, Olaf Pongs, Bert L de Groot, Ulrich Zachariae

Publikováno v: PLoS ONE, Vol 7, Iss 7, p e41023 (2012)

K(+) channels control transmembrane action potentials by gating open or closed in response to external stimuli. Inactivation gating, involving a conformational change at the K(+) selectivity filter, has recently been recognized as a major K(+) channe

Externí odkaz: https://doaj.org/article/09da7d2423f74e799d57e69776b32492

Allosteric Features of KCNQ1 Gating Revealed by Alanine Scanning Mutagenesis

Autor: Li-Juan Ma, Vitya Vardanyan, Iris Ohmert

Publikováno v: Biophysical Journal. 100(4):885-894

Controlled opening and closing of an ion-selective pathway in response to changes of membrane potential is a fundamental feature of voltage-gated ion channels. In recent decades, various details of this process have been revealed with unprecedented p

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07d997281704190ede397b8803a99493

Coupling of activation and inactivation gate in a K+-channel: potassium and ligand sensitivity

Autor: Vitya Vardanyan, Sönke Hornig, Karin Giller, Phanindra Velisetty, Olaf Pongs, Marc Baldus, Iris Ohmert, Stefan Becker, Robert Schneider, Christian Ader

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 delinea

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aae88c9429920dc213e47e53a49382b3
https://dspace.library.uu.nl/handle/1874/44415

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

Autor: Christian Ader, Phanindra Velisetty, Adam Lange, Dirk Trauner, Olaf Pongs, Sönke Hornig, Robert Schneider, Erica M. Wilson, Karin Giller, Stefan Becker, Marc Baldus, Marie-France Martin-Eauclaire, Iris Ohmert

Publikováno v: Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, Nature Publishing Group, 2008, 15 (6), pp.605-12. ⟨10.1038/nsmb.1430⟩
Nature Structural and Molecular Biology, 2008, 15 (6), pp.605-12. ⟨10.1038/nsmb.1430⟩

International audience; 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

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e543247b92cfbf2bfb4da898c94b3c5a
https://hal.archives-ouvertes.fr/hal-00396760

A Molecular Switch Driving Inactivation in the Cardiac K+ Channel hERG

Autor: Gert Vriend, David A. Köpfer, Olaf Pongs, Ulrike Hahn, Bert L. de Groot, Ulrich Zachariae, Iris Ohmert

Publikováno v: PLoS ONE, Vol 7, Iss 7, p e41023 (2012)
PLoS One, 7
PLoS One, 7, 7
Kopfer, D A, Hahn, U, Ohmert, I, Vriend, G, Pongs, O, de Groot, B L & Zachariae, U 2012, ' A Molecular Switch Driving Inactivation in the Cardiac K+ Channel hERG ', PLoS ONE, vol. 7, no. 7, e41023 . https://doi.org/10.1371/journal.pone.0041023
PLoS One
PLoS ONE

Contains fulltext : 103432.pdf (Publisher’s version ) (Open Access) K(+) channels control transmembrane action potentials by gating open or closed in response to external stimuli. Inactivation gating, involving a conformational change at the K(+) s

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4b91701e99688117110cee2efac50c0f
https://doi.org/10.1371/journal.pone.0041023