Publication: Sodium channel activators: model of binding inside the pore and a possible

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Title	Sodium channel activators: model of binding inside the pore and a possible
Authors/Editors*	Denis B. Tikhonov and Boris S. Zhorov
Where published*	FEBS Letters
How published*	Journal
Year*	2005
Volume	579
Number	20
Pages	4207-12
Publisher
Keywords
Link	http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=16083886&query_hl=1&itool=pubmed_docsum
Abstract	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.