What defines a gate? The enigmas of K+ channel structural mechanics
Thanh-Hao Nguyen1, Xue Zhang2, Martina Klejchova1
1Laboratory of Plant Physiology and Biophysics, School of Molecular Biosciences, Bower Building, University of Glasgow, Glasgow G12 8QQ, UK.
Abstract:
Potassium (K+) channels vary in shape and size. Commonly, they form a functional pore through the membrane as an assembly of four subunits. For the predominant family of K+ channels at the plant plasma membrane, each subunit comprises a polypeptide of six transmembrane helices with a canonical voltage-sensor domain fused to a pair of pore-lining helices. These constructs give rise to a wide range of behaviours that are nonetheless 'hard-wired' within the channel protein structure. With cryo-EM data now available for four arabidopsis (Arabidopsis thaliana) K+ channels, it nonetheless remains an enigma how the structural mechanics give rise to channels that open-or gate-for K+ flux across widely differing voltages and how ligands, especially K+ itself, regulate this flux.
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