Hydrophobic gating in BK channels

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Kinetic Gating Mechanisms for Bk Channels

Large conductance calcium-activated K ϩ channels, also referred to as " BK " or " maxi K " channels because of their big single-channel conductance (‫ف‬ 300 pS in symmetrical 150 mM KCl) are widely distributed in many different tissues (Latorre, 1994; Kaczorowski et al., 1996). A signature feature of BK channels, in addition to their high K ϩ selectivity and conductance, is that they are activa...

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Gating Mechanism of BK (Slo1) Channels

Large conductance calciumand voltage-activated K channels (Slo1), also referred to as “BK” or “maxi K” channels because of their high single channel conductance (250–300 pS in symmetrical 150 mM KCl), are widely distributed in many different tissues (Kaczorowski et al., 1996). A signature feature of BK channels, in addition to their high K selectivity and conductance, is that they are activated...

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Relationship between Pore Occupancy and Gating in BK Potassium Channels

Permeant ions can have significant effects on ion channel conformational changes. To further understand the relationship between ion occupancy and gating conformational changes, we have studied macroscopic and single-channel gating of BK potassium channels with different permeant monovalent cations. While the slopes of the conductance-voltage curve were reduced with respect to potassium for all...

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Principles of conduction and hydrophobic gating in K+ channels.

We present the first atomic-resolution observations of permeation and gating in a K(+) channel, based on molecular dynamics simulations of the Kv1.2 pore domain. Analysis of hundreds of simulated permeation events revealed a detailed conduction mechanism, resembling the Hodgkin-Keynes "knock-on" model, in which translocation of two selectivity filter-bound ions is driven by a third ion; formati...

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Deletion of cytosolic gating ring decreases gate and voltage sensor coupling in BK channels

Large conductance Ca2+-activated K+ channels (BK channels) gate open in response to both membrane voltage and intracellular Ca2+ The channel is formed by a central pore-gate domain (PGD), which spans the membrane, plus transmembrane voltage sensors and a cytoplasmic gating ring that acts as a Ca2+ sensor. How these voltage and Ca2+ sensors influence the common activation gate, and interact with...

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ژورنال

عنوان ژورنال: Nature Communications

سال: 2018

ISSN: 2041-1723

DOI: 10.1038/s41467-018-05970-3