{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,12]],"date-time":"2026-07-12T10:06:29Z","timestamp":1783850789606,"version":"3.55.0"},"reference-count":52,"publisher":"Wiley","issue":"8","license":[{"start":{"date-parts":[[2012,4,4]],"date-time":"2012-04-04T00:00:00Z","timestamp":1333497600000},"content-version":"vor","delay-in-days":3,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2012,4]]},"abstract":"<jats:p>Scorpion toxins targeting voltage\u2010gated sodium (Na<jats:sub>V<\/jats:sub>) channels are peptides that comprise 60\u201376 amino acid residues cross\u2010linked by four disulfide bridges. These toxins can be divided in two groups (\u03b1 and \u03b2 toxins), according to their binding properties and mode of action. The scorpion \u03b1\u2010toxin Ts2, previously described as a \u03b2\u2010toxin, was purified from the venom of <jats:italic>Tityus\u2003serrulatus<\/jats:italic>, the most dangerous Brazilian scorpion. In this study, seven mammalian Na<jats:sub>V<\/jats:sub> channel isoforms (rNa<jats:sub>V<\/jats:sub>1.2, rNa<jats:sub>V<\/jats:sub>1.3, rNa<jats:sub>V<\/jats:sub>1.4, hNa<jats:sub>V<\/jats:sub>1.5, mNa<jats:sub>V<\/jats:sub>1.6, rNa<jats:sub>V<\/jats:sub>1.7 and rNa<jats:sub>V<\/jats:sub>1.8) and one insect Na<jats:sub>V<\/jats:sub> channel isoform (DmNa<jats:sub>V<\/jats:sub>1) were used to investigate the subtype specificity and selectivity of Ts2. The electrophysiology assays showed that Ts2 inhibits rapid inactivation of Na<jats:sub>V<\/jats:sub>1.2, Na<jats:sub>V<\/jats:sub>1.3, Na<jats:sub>V<\/jats:sub>1.5, Na<jats:sub>V<\/jats:sub>1.6 and Na<jats:sub>V<\/jats:sub>1.7, but does not affect Na<jats:sub>V<\/jats:sub>1.4, Na<jats:sub>V<\/jats:sub>1.8 or DmNa<jats:sub>V<\/jats:sub>1. Interestingly, Ts2 significantly shifts the voltage dependence of activation of Na<jats:sub>V<\/jats:sub>1.3 channels. The 3D structure of this toxin was modeled based on the high sequence identity (72%) shared with Ts1, another <jats:italic>T.\u2003serrulatus<\/jats:italic> toxin. The overall fold of the Ts2 model consists of three \u03b2\u2010strands and one \u03b1\u2010helix, and is arranged in a triangular shape forming a cysteine\u2010stabilized \u03b1\u2010helix\/\u03b2\u2010sheet (CS\u03b1\u03b2) motif.<\/jats:p><jats:p><jats:bold>Database<\/jats:bold> Model data are available in the PMDB under accession number <jats:ext-link xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" xlink:href=\"http:\/\/mi.caspur.it\/PMDB\/\">PM0077533<\/jats:ext-link>.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2012.08545.x","type":"journal-article","created":{"date-parts":[[2012,2,22]],"date-time":"2012-02-22T19:39:17Z","timestamp":1329939557000},"page":"1495-1504","source":"Crossref","is-referenced-by-count":41,"title":["Investigation of the relationship between the structure and function of Ts2, a neurotoxin from <i>Tityus\u2003serrulatus<\/i> venom"],"prefix":"10.1111","volume":"279","author":[{"given":"Camila T.","family":"Cologna","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steve","family":"Peigneur","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Joane K.","family":"Rustiguel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"M. 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