Gating energetics of a voltage-dependent K+ channel pore domain

2017 ◽  
Vol 38 (16) ◽  
pp. 1472-1478 ◽  
Author(s):  
Greg Starek ◽  
J. Alfredo Freites ◽  
Simon Bernèche ◽  
Douglas J. Tobias
Keyword(s):  
K Channel ◽  
Channel Pore ◽  
Voltage Dependent ◽  
Pore Domain

scholarly journals Tethered Peptide Neurotoxins Facilitate Biophysical Study and Reveal Two Voltage-dependent Blocking Mechanisms for SAK1 Toxins in the K+ Channel Pore

2020 ◽  
Vol 118 (3) ◽  
pp. 110a-111a
Author(s):  
Ruiming Zhao ◽  
Hui Dai ◽  
Netanel Mendelman ◽  
Jordan H. Chill ◽  
Steve A. Goldstein
Keyword(s):  
K Channel ◽  
Channel Pore ◽  
Voltage Dependent ◽  
Biophysical Study ◽  
Blocking Mechanisms

scholarly journals Interaction of local anesthetics with the K+channel pore domain

Channels ◽  
2013 ◽  
Vol 7 (3) ◽  
pp. 182-193 ◽  
Author(s):  
Noel W. Gray ◽  
Boris S. Zhorov ◽  
Edward G. Moczydlowski
Keyword(s):  
Local Anesthetics ◽  
K Channel ◽  
Channel Pore ◽  
Pore Domain

scholarly journals Interactive domains between pore loops of the yeast K+ channel TOK1 associate with extracellular K+ sensitivity

2006 ◽  
Vol 393 (3) ◽  
pp. 645-655 ◽  
Author(s):  
Ingela Johansson ◽  
Michael R. Blatt
Keyword(s):  
Double Mutant ◽  
K Channel ◽  
Wild Type ◽  
Long Distance ◽  
Voltage Dependent ◽  
Polypeptide Backbone ◽  
K Concentration ◽  
Pore Domain ◽  
Distance Interaction ◽  
Pore Domains

Gating of the outward-rectifying K+ channel TOK1 of Saccharomyces cerevisiae is controlled by membrane voltage and extracellular K+ concentration. Previous studies identified two kinetically distinct effects of K+, and site-mutagenic analysis associated these K+-dependencies with domains of the extracellular turrets of the channel protein. We have mapped the TOK1 pore domains to extant K+ channel crystal structures to target additional residues contributing to TOK1 gating. Leu270, located in the first pore domain of TOK1, was found to be critical for gating and its K+ sensitivity. Analysis of amino acid substitutions indicated that spatial position of the polypeptide backbone is a primary factor determining gating sensitivity to K+. The strongest effects, with L270Y, L270F and L270W, led to more than a 30-fold decrease in apparent K+ affinity and an inversion in the apparent K+-dependence of voltage-dependent gating compared with the wild-type current. A partial rescue of wild-type gating was obtained on substitution in the second pore domain with the double mutant L270D/A428Y. These, and additional results, demarcate extracellular domains that are associated with the K+-sensitivity of TOK1 and they offer primary evidence for a synergy in gating between the two pore domains of TOK1, demonstrating an unexpected degree of long-distance interaction across the mouth of the K+ channel.

scholarly journals Conformational Flexibility of the hERG K+ Channel Pore Domain

2010 ◽  
Vol 98 (3) ◽  
pp. 120a
Author(s):  
Anna Weinzinger ◽  
Kirsten Knape ◽  
Sören J. Wacker ◽  
Lars Boukharta ◽  
Bert L. de Groot
Keyword(s):  
Conformational Flexibility ◽  
K Channel ◽  
Channel Pore ◽  
Pore Domain
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