{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T13:22:15Z","timestamp":1791638535676,"version":"4.3.4"},"reference-count":71,"publisher":"Wiley","issue":"12","license":[{"start":{"date-parts":[[2004,5,26]],"date-time":"2004-05-26T00:00:00Z","timestamp":1085529600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["European Journal of Biochemistry"],"published-print":{"date-parts":[[2004,6]]},"abstract":"<jats:p>Cn12 isolated from the venom of the scorpion <jats:italic>Centruroides noxius<\/jats:italic> has 67 amino\u2010acid residues, closely packed with four disulfide bridges. Its primary structure and disulfide bridges were determined. Cn12 is not lethal to mammals and arthropods <jats:italic>in vivo<\/jats:italic> at doses up to 100\u2003\u03bcg per animal. Its 3D structure was determined by proton NMR using 850 distance constraints, 36 \u03c6 angles derived from 36 coupling constants obtained by two different methods, and 22 hydrogen bonds. The overall structure has a two and half turn \u03b1\u2010helix (residues 24\u201332), three strands of antiparallel \u03b2\u2010sheet (residues 2\u20134, 37\u201340 and 45\u201348), and a type II turn (residues 41\u201344). The amino\u2010acid sequence of Cn12 resembles the \u03b2 scorpion toxin class, although patch\u2010clamp experiments showed the induction of supplementary slow inactivation of Na<jats:sup>+<\/jats:sup> channels in F\u201011 cells (mouse neuroblastoma N18TG\u20102\u2003\u00d7\u2003rat DRG2), which means that it behaves more like an \u03b1 scorpion toxin. This behaviour prompted us to analyse Na<jats:sup>+<\/jats:sup> channel binding sites using information from 112 Na<jats:sup>+<\/jats:sup> channel gene clones available in the literature, focusing on the extracytoplasmic loops of the S5\u2013S6 transmembrane segments of domain I and the S3\u2013S4 segments of domain IV, sites considered to be responsible for binding \u03b1 scorpion toxins.<\/jats:p>","DOI":"10.1111\/j.1432-1033.2004.04181.x","type":"journal-article","created":{"date-parts":[[2004,6,4]],"date-time":"2004-06-04T13:16:21Z","timestamp":1086354981000},"page":"2504-2516","source":"Crossref","is-referenced-by-count":20,"title":["NMR solution structure of Cn12, a novel peptide from the Mexican scorpion <i>Centruroides noxius<\/i> with a typical \u03b2\u2010toxin sequence but with \u03b1\u2010like physiological activity"],"prefix":"10.1111","volume":"271","author":[{"given":"Federico","family":"del 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