Thermodynamic characteristics of gating mechanisms of fast potassium channels of snall neuron somatic membrane

1984 ◽  
Vol 15 (6) ◽  
pp. 409-416
Author(s):  
I. S. Magura ◽  
N. B. Prevarskaya ◽  
V. A. Dub
Keyword(s):  
Potassium Channels ◽  
Thermodynamic Characteristics ◽  
Somatic Membrane ◽  
Gating Mechanisms

scholarly journals Gating Mechanisms of Cardiac and Neuronal KCNQ Potassium Channels

2020 ◽  
Vol 118 (3) ◽  
pp. 264a
Author(s):  
Nien-Du Yang ◽  
Alex Dou ◽  
Po Wei Kang ◽  
Panpan Hou ◽  
Kelli McFarland White ◽  
...  
Keyword(s):  
Potassium Channels ◽  
Gating Mechanisms

scholarly journals K2P channel C-type gating involves asymmetric selectivity filter order-disorder transitions

2020 ◽  
Vol 6 (44) ◽  
pp. eabc9174
Author(s):  
Marco Lolicato ◽  
Andrew M. Natale ◽  
Fayal Abderemane-Ali ◽  
David Crottès ◽  
Sara Capponi ◽  
...  
Keyword(s):  
Potassium Channels ◽  
Conformational Changes ◽  
Structural Changes ◽  
Selectivity Filter ◽  
Anomalous Scattering ◽  
X Ray Crystallography ◽  
Gating Mechanisms ◽  
Cellular Excitability ◽  
Ion Binding Sites ◽  
Channel Modulator

K2P potassium channels regulate cellular excitability using their selectivity filter (C-type) gate. C-type gating mechanisms, best characterized in homotetrameric potassium channels, remain controversial and are attributed to selectivity filter pinching, dilation, or subtle structural changes. The extent to which such mechanisms control C-type gating of innately heterodimeric K2Ps is unknown. Here, combining K2P2.1 (TREK-1) x-ray crystallography in different potassium concentrations, potassium anomalous scattering, molecular dynamics, and electrophysiology, we uncover unprecedented, asymmetric, potassium-dependent conformational changes that underlie K2P C-type gating. These asymmetric order-disorder transitions, enabled by the K2P heterodimeric architecture, encompass pinching and dilation, disrupt the S1 and S2 ion binding sites, require the uniquely long K2P SF2-M4 loop and conserved “M3 glutamate network,” and are suppressed by the K2P C-type gate activator ML335. These findings demonstrate that two distinct C-type gating mechanisms can operate in one channel and underscore the SF2-M4 loop as a target for K2P channel modulator development.

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