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The Na Channel Voltage Sensor Associated with Inactivation Is Localized to the External Charged Residues of Domain IV, S4
1999
Biophysical Journal
Site-3 toxins have been shown to inhibit a component of gating charge (33% of maximum gating charge, Q max ) in native cardiac Na channels that has been identified with the open-to-inactivated state kinetic transition. To investigate the role of the three outermost arginine amino acid residues in segment 4 domain IV (R1, R2, R3) in gating charge inhibited by site-3 toxins, we recorded ionic and gating currents from human heart Na channels with mutations of the outermost arginines (R1C, R1Q,
doi:10.1016/s0006-3495(99)76929-8
pmid:10423423
pmcid:PMC1300369
fatcat:a6f6wtoa4nc3nedlgimnftjqky