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Characterizing Na+/K+ Permeation Rates through the Bacterial NavAb Sodium Channel
2014
Biophysical Journal
resolution structural data on human sodium channels, the publication of a number of crystal structures of related, bacterial voltage-gated sodium channel in the last 2 years has offered the opportunity to explore the mechanism of entry and location of binding sodium channel blockers. Here, molecular dynamics simulations were used to determine the binding site of two channel blockers, benzocaine and phenytoin in the bacterial channel NavAb. We find that that binding involves nonspecific
doi:10.1016/j.bpj.2013.11.774
fatcat:3ar2sq7jonccbpagth24uvtb74