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Voltage-gated sodium channels viewed through a structural biology lens.pdf
Available online at
ScienceDirect
Voltage-gated sodium channels viewed through a
structural biology lens Thomas Clairfeuille1, Hui Xu1, Christopher M Koth and
Jian Payandeh
Voltage-gated sodium (Nav) channels initiate and propagate action potentials in excitable cells, and are frequently dysregulated or mutated in human disease. Despite decades of intense physiological and biophysical research, eukaryotic Nav channels have so far eluded high-resolution structure determination because of their biochemical complexity. Recently, simpler bacterial voltage-gated sodium (BacNav) channels have provided templates to understand the structural basis of voltage-dependent activation, inactivation, ion selectivity, and drug block in eukaryotic Nav and related voltage-gated calcium (Cav) channels. Further breakthroughs employing BacNav channels have also enabled visualization of bound small molecule modulators that can guide the rational design of next generation therapeutics. This review will highlight the emerging structural biology of BacNav channels and its contribution to our understanding of the gating, ion selectivity, and pharmacological regulation of eukaryotic Nav (and Cav) channels.
Address Department of Structural Biology, Genentech Inc., South San Francisco, CA 94080, USA
Corresponding author: Payandeh, Jian (payandeh.jian@) 1 T.C. and H.X. contributed equally to this work.
Current Opinion in Structural Biology 2017, 45:74–84 This review comes from a themed issue on Membranes Edited by Martin Caffrey and David Drew
/10.1016/j.sbi.2016.11.022 0959-440/# 2016 Elsevier Ltd. All rights reserved.
Introduction Voltage-gated sodium (Nav), calcium (Cav), and potassium (Kv) channels form a superfamily of ion channels that open and close ion-selective pores in response to small changes in membrane potential [1,2]. High-resolution structures of homotetrameric K+ channels have been available for nearly two decades [3,4,5,6], but eukaryotic Nav and Cav channels lack the
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