{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,27]],"date-time":"2026-09-27T08:36:30Z","timestamp":1790498190635,"version":"4.1.0"},"reference-count":37,"publisher":"Rockefeller University Press","issue":"3","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2007,9,1]]},"abstract":"<jats:p>Several naturally occurring polypeptide neurotoxins target specific sites on the voltage-gated sodium channels. Of these, the gating modifier toxins alter the behavior of the sodium channels by stabilizing transient intermediate states in the channel gating pathway. Here we have used an integrated approach that combines electrophysiological and spectroscopic measurements to determine the structural rearrangements modified by the \u03b2-scorpion toxin Ts1. Our data indicate that toxin binding to the channel is restricted to a single binding site on domain II voltage sensor. Analysis of Cole-Moore shifts suggests that the number of closed states in the activation sequence prior to channel opening is reduced in the presence of toxin. Measurements of charge\u2013voltage relationships show that a fraction of the gating charge is immobilized in Ts1-modified channels. Interestingly, the charge\u2013voltage relationship also shows an additional component at hyperpolarized potentials. Site-specific fluorescence measurements indicate that in presence of the toxin the voltage sensor of domain II remains trapped in the activated state. Furthermore, the binding of the toxin potentiates the activation of the other three voltage sensors of the sodium channel to more hyperpolarized potentials. These findings reveal how the binding of \u03b2-scorpion toxin modifies channel function and provides insight into early gating transitions of sodium channels.<\/jats:p>","DOI":"10.1085\/jgp.200609719","type":"journal-article","created":{"date-parts":[[2007,8,14]],"date-time":"2007-08-14T00:40:41Z","timestamp":1187052041000},"page":"257-268","update-policy":"https:\/\/doi.org\/10.1085\/jgp.crossmarkpolicy","source":"Crossref","is-referenced-by-count":71,"title":["\u03b2-Scorpion Toxin Modifies Gating Transitions in All Four Voltage Sensors of the Sodium Channel"],"prefix":"10.1085","volume":"130","author":[{"given":"Fabiana V.","family":"Campos","sequence":"first","affiliation":[{"name":"1Institute for Molecular Pediatric Sciences and Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637"},{"name":"2Department of Biochemistry and Immunology, Instituto de Cie\u0302ncias Biolo\u0301gicas, Universidade Federal de Minas Gerais, Belo Horizonte, Minas Gerais, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Baron","family":"Chanda","sequence":"additional","affiliation":[{"name":"3Department of Physiology, University of Wisconsin-Madison, Madison, WI 53706"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paulo S.L.","family":"Beira\u0303o","sequence":"additional","affiliation":[{"name":"2Department of Biochemistry and Immunology, Instituto de Cie\u0302ncias Biolo\u0301gicas, Universidade Federal de Minas Gerais, Belo Horizonte, Minas Gerais, Brazil"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Francisco","family":"Bezanilla","sequence":"additional","affiliation":[{"name":"1Institute for Molecular Pediatric Sciences and Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"291","published-online":{"date-parts":[[2007,8,13]]},"reference":[{"key":"2023072920390385400_BIB1","doi-asserted-by":"crossref","first-page":"567","DOI":"10.1085\/jgp.70.5.567","volume":"70","year":"1977","journal-title":"J. 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