title: Site-3 sea anemone toxins: molecular probes of gating mechanisms in voltage-dependent sodium channels.
abstract: Sea anemone toxins, whose biological function is the capture of marine prey, are invaluable tools for studying the structure and function of mammalian voltage-gated sodium channels. Their high degree of specificity and selectivity have allowed for detailed analysis of inactivation gating and assignment of molecular entities responsible for this process. Because of their ability to discriminate among channel isoforms, and their high degree of structural conservation, these toxins could serve as important lead compounds for future pharmaceutical design.
authors.affiliation: Department of Biochemistry, School of Medicine and Biomedical Sciences, State University of New York, 3435 Main St. Buffalo, NY 14214, USA.
authors.forename: Jaime J
authors.initials: JJ
authors.lastname: Smith
authors.forename: Kenneth M
authors.initials: KM
authors.lastname: Blumenthal
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D003064:Cnidarian Venoms / Q000235:genetics* / Q000494:pharmacology*; D006801:Humans; D015640:Ion Channel Gating / Q000187:drug effects / Q000502:physiology; D015335:Molecular Probes; D008969:Molecular Sequence Data; D012615:Sea Anemones; D015222:Sodium Channels / Q000187:drug effects*
chemical_list: D003064:Cnidarian Venoms; D015335:Molecular Probes; D015222:Sodium Channels