title: Probing gating mechanisms of sodium channels using pore blockers.
abstract: Several classes of small molecules and peptides bind at the central pore of voltage-gated sodium channels either from the extracellular or intracellular side of the membrane and block ion conduction through the pore. Biophysical studies that shed light on the chemical nature, accessibility, and kinetics of binding of these naturally occurring and synthetic compounds reveal a wealth of information about how these channels gate. Here, we discuss insights into the structural underpinnings of gating of the channel pore and its coupling to the voltage sensors obtained from pore blockers including site 1 neurotoxins and local anesthetics.
authors.affiliation: Department of Neuroscience, University of Wisconsin, Madison, WI, USA.
authors.forename: Marcel P
authors.initials: MP
authors.lastname: Goldschen-Ohm
authors.forename: Baron
authors.initials: B
authors.lastname: Chanda
mesh_terms: D000200:Action Potentials; D000818:Animals; D002462:Cell Membrane / Q000187:drug effects* / Q000378:metabolism; D006801:Humans; D015640:Ion Channel Gating / Q000187:drug effects*; D007700:Kinetics; D015394:Molecular Structure; D011487:Protein Conformation; D015398:Signal Transduction / Q000187:drug effects; D012964:Sodium / Q000378:metabolism*; D026941:Sodium Channel Blockers / Q000737:chemistry / Q000494:pharmacology*; D015222:Sodium Channels / Q000737:chemistry / Q000187:drug effects* / Q000378:metabolism; D013329:Structure-Activity Relationship
chemical_list: D026941:Sodium Channel Blockers; D015222:Sodium Channels; D012964:Sodium