期刊
FEBS LETTERS
卷 579, 期 20, 页码 4207-4212出版社
WILEY
DOI: 10.1016/j.febslet.2005.07.017
关键词
batrachotoxin; veratridine; energy minimization; Monte Carlo minimization; channel gating; channel block; ion permeation
Sodium channel activators, batrachotoxin and veratridine, cause sodium channels to activate easier and stay open longer than normal channels. Traditionally, this was explained by an allosteric mechanism. However, increasing evidence suggests that activators can bind inside the pore. Here, we model the open sodium channel with activators and propose a novel mechanism of their action. The activator-bound channel retains a hydrophilic pathway for ions between the ligand and conserved asparagine in segment S6 of repeat II. One end of the activator approaches the selectivity filter, decreasing the channel conductance and selectivity. The opposite end reaches the gate stabilizing it in the open state. (c) 2005 Published by Elsevier B.V. on behalf of the Federation of European Biochemical Societies.
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