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The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation.

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The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation. / Zachariae, Ulrich; Schneider, Robert; Velisetty, Phanindra; Lange, Adam; Seeliger, Daniel; Wacker, Sören J; Karimi-Nejad, Yasmin; Vriend, Gert; Becker, Stefan; Pongs, Olaf; Baldus, Marc; Groot, de; Bert, L.

In: STRUCTURE, Vol. 16, No. 5, 5, 2008, p. 747-754.

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

Harvard

Zachariae, U, Schneider, R, Velisetty, P, Lange, A, Seeliger, D, Wacker, SJ, Karimi-Nejad, Y, Vriend, G, Becker, S, Pongs, O, Baldus, M, Groot, D & Bert, L 2008, 'The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation.', STRUCTURE, vol. 16, no. 5, 5, pp. 747-754. <http://www.ncbi.nlm.nih.gov/pubmed/18462679?dopt=Citation>

APA

Zachariae, U., Schneider, R., Velisetty, P., Lange, A., Seeliger, D., Wacker, S. J., Karimi-Nejad, Y., Vriend, G., Becker, S., Pongs, O., Baldus, M., Groot, D., & Bert, L. (2008). The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation. STRUCTURE, 16(5), 747-754. [5]. http://www.ncbi.nlm.nih.gov/pubmed/18462679?dopt=Citation

Vancouver

Zachariae U, Schneider R, Velisetty P, Lange A, Seeliger D, Wacker SJ et al. The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation. STRUCTURE. 2008;16(5):747-754. 5.

Bibtex

@article{2e50452edd8c4f648099845b96ababec,
title = "The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation.",
abstract = "Recently, a solid-state NMR study revealed that scorpion toxin binding leads to conformational changes in the selectivity filter of potassium channels. The exact nature of the conformational changes, however, remained elusive. We carried out all-atom molecular dynamics simulations that enabled us to cover the complete pathway of toxin approach and binding, and we validated our simulation results by using solid-state NMR data and electrophysiological measurements. Our structural model revealed a mechanism of cooperative toxin-induced conformational changes that accounts both for the signal changes observed in solid-state NMR and for the tight interaction between KcsA-Kv1.3 and Kaliotoxin. We show that this mechanism is structurally and functionally closely related to recovery from C-type inactivation. Furthermore, our simulations indicate heterogeneity in the binding modes of Kaliotoxin, which might serve to enhance its affinity for KcsA-Kv1.3 further by entropic stabilization.",
author = "Ulrich Zachariae and Robert Schneider and Phanindra Velisetty and Adam Lange and Daniel Seeliger and Wacker, {S{\"o}ren J} and Yasmin Karimi-Nejad and Gert Vriend and Stefan Becker and Olaf Pongs and Marc Baldus and de Groot and L Bert",
year = "2008",
language = "Deutsch",
volume = "16",
pages = "747--754",
journal = "STRUCTURE",
issn = "0969-2126",
publisher = "Cell Press",
number = "5",

}

RIS

TY - JOUR

T1 - The molecular mechanism of toxin-induced conformational changes in a potassium channel: relation to C-type inactivation.

AU - Zachariae, Ulrich

AU - Schneider, Robert

AU - Velisetty, Phanindra

AU - Lange, Adam

AU - Seeliger, Daniel

AU - Wacker, Sören J

AU - Karimi-Nejad, Yasmin

AU - Vriend, Gert

AU - Becker, Stefan

AU - Pongs, Olaf

AU - Baldus, Marc

AU - Groot, de

AU - Bert, L

PY - 2008

Y1 - 2008

N2 - Recently, a solid-state NMR study revealed that scorpion toxin binding leads to conformational changes in the selectivity filter of potassium channels. The exact nature of the conformational changes, however, remained elusive. We carried out all-atom molecular dynamics simulations that enabled us to cover the complete pathway of toxin approach and binding, and we validated our simulation results by using solid-state NMR data and electrophysiological measurements. Our structural model revealed a mechanism of cooperative toxin-induced conformational changes that accounts both for the signal changes observed in solid-state NMR and for the tight interaction between KcsA-Kv1.3 and Kaliotoxin. We show that this mechanism is structurally and functionally closely related to recovery from C-type inactivation. Furthermore, our simulations indicate heterogeneity in the binding modes of Kaliotoxin, which might serve to enhance its affinity for KcsA-Kv1.3 further by entropic stabilization.

AB - Recently, a solid-state NMR study revealed that scorpion toxin binding leads to conformational changes in the selectivity filter of potassium channels. The exact nature of the conformational changes, however, remained elusive. We carried out all-atom molecular dynamics simulations that enabled us to cover the complete pathway of toxin approach and binding, and we validated our simulation results by using solid-state NMR data and electrophysiological measurements. Our structural model revealed a mechanism of cooperative toxin-induced conformational changes that accounts both for the signal changes observed in solid-state NMR and for the tight interaction between KcsA-Kv1.3 and Kaliotoxin. We show that this mechanism is structurally and functionally closely related to recovery from C-type inactivation. Furthermore, our simulations indicate heterogeneity in the binding modes of Kaliotoxin, which might serve to enhance its affinity for KcsA-Kv1.3 further by entropic stabilization.

M3 - SCORING: Zeitschriftenaufsatz

VL - 16

SP - 747

EP - 754

JO - STRUCTURE

JF - STRUCTURE

SN - 0969-2126

IS - 5

M1 - 5

ER -