{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,10]],"date-time":"2026-10-10T17:37:02Z","timestamp":1791653822010,"version":"4.3.4"},"reference-count":68,"publisher":"Portland Press Ltd.","issue":"3","license":[{"start":{"date-parts":[[2019,7,25]],"date-time":"2019-07-25T00:00:00Z","timestamp":1564012800000},"content-version":"vor","delay-in-days":2245,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2013,6,1]]},"abstract":"<jats:p>The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new scorpion venom-derived K+ channel toxin (named \u03bb-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2+ release measurements and electrophysiological recordings. \u03bb-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel \u03b2-sheet and a 310-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2+ release channels\/ryanodine receptors, which is remarkably different from the previously known scorpion venom ICK peptides. The removal of two C-terminal residues of \u03bb-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of \u03bb-MeuKTx-1. The presence of a functional dyad in \u03bb-MeuKTx-1 supports functional convergence among scorpion venom peptides with different folds. Furthermore, similarities in precursor organization, exon\u2013intron structure, 3D-fold and function suggest that scorpion venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural and functional characterizations of the first scorpion venom ICK toxin with K+ channel-blocking activity sheds light on functionally divergent and convergent evolution of this conserved scaffold of ancient origin.<\/jats:p>","DOI":"10.1042\/bsr20130052","type":"journal-article","created":{"date-parts":[[2013,5,31]],"date-time":"2013-05-31T09:04:53Z","timestamp":1369991093000},"update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":58,"title":["Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold"],"prefix":"10.1042","volume":"33","author":[{"given":"Bin","family":"Gao","sequence":"first","affiliation":[{"name":"Group of Animal Innate Immunity, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, 1 Beichen West Road, Chaoyang District, Beijing 100101, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peta\u00a0J.","family":"Harvey","sequence":"additional","affiliation":[{"name":"Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David\u00a0J.","family":"Craik","sequence":"additional","affiliation":[{"name":"Institute for Molecular Bioscience, University of Queensland, Brisbane, Queensland 4072, Australia"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michel","family":"Ronjat","sequence":"additional","affiliation":[{"name":"Grenoble Institut des Neurosciences, Inserm U836, \u00e9quipe 3, LabEx Ion Channel Science and Therapeutics, B\u00e2t. Edmond J. Safra, Universit\u00e9 Joseph Fourier, Site Sant\u00e9 de la Tronche, BP 170, 38042 Grenoble Cedex 9, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michel","family":"De Waard","sequence":"additional","affiliation":[{"name":"Grenoble Institut des Neurosciences, Inserm U836, \u00e9quipe 3, LabEx Ion Channel Science and Therapeutics, B\u00e2t. Edmond J. Safra, Universit\u00e9 Joseph Fourier, Site Sant\u00e9 de la Tronche, BP 170, 38042 Grenoble Cedex 9, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shunyi","family":"Zhu","sequence":"additional","affiliation":[{"name":"Group of Animal Innate Immunity, State Key Laboratory of Integrated Management of Pest Insects and Rodents, Institute of Zoology, Chinese Academy of Sciences, 1 Beichen West Road, Chaoyang District, Beijing 100101, People's Republic of China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2013,6,27]]},"reference":[{"key":"2021111618153149800_B1","first-page":"557","article-title":"Potassium channels: molecular defects, diseases, and therapeutic opportunities","volume":"52","author":"Shieh","year":"2000","journal-title":"Pharmacol. 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