Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif

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dc.contributor.author Smith, Jennifer en_US
dc.contributor.author Hill, Justine en_US
dc.contributor.author Little, Michelle en_US
dc.contributor.author Nicholson, Graham en_US
dc.contributor.author Alewood, Paul en_US
dc.contributor.author King, Glenn en_US
dc.contributor.editor en_US
dc.date.accessioned 2012-10-12T03:33:24Z
dc.date.available 2012-10-12T03:33:24Z
dc.date.issued 2011 en_US
dc.identifier 2010003227 en_US
dc.identifier.citation Smith Jennifer et al. 2011, 'Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif', National Academy of Sciences, vol. 108, no. 26, pp. 10478-10483. en_US
dc.identifier.issn 0027-8424 en_US
dc.identifier.other C1 en_US
dc.identifier.uri http://hdl.handle.net/10453/18123
dc.description.abstract The three-disulfide inhibitor cystine knot (ICK) motif is a fold common to venom peptides from spiders, scorpions, and aquatic cone snails. Over a decade ago it was proposed that the ICK motif is an elaboration of an ancestral two-disulfide fold coined the disulfide-directed beta-hairpin (DDH). Here we report the isolation, characterization, and structure of a novel toxin [U(1)-liotoxin-Lw1a (U(1)-LITX-Lw1a)] from the venom of the scorpion Liocheles waigiensis that is the first example of a native peptide that adopts the DDH fold. U(1)-LITX-Lw1a not only represents the discovery of a missing link in venom protein evolution, it is the first member of a fourth structural fold to be adopted by scorpion-venom peptides. Additionally, we show that U(1)-LITX-Lw1a has potent insecticidal activity across a broad range of insect pest species, thereby providing a unique structural scaffold for bioinsecticide development. en_US
dc.language en_US
dc.publisher National Academy of Sciences en_US
dc.relation.hasversion Accepted manuscript version en_US
dc.relation.isbasedon http://dx.doi.org/10.1073/pnas.1103501108 en_US
dc.title Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif en_US
dc.parent Proceedings Of The National Academy Of Sciences Of The United States Of America en_US
dc.journal.volume 108 en_US
dc.journal.number 26 en_US
dc.publocation Washington, DC USA en_US
dc.identifier.startpage 10478 en_US
dc.identifier.endpage 10483 en_US
dc.cauo.name SCI.Medical and Molecular Biosciences en_US
dc.conference Verified OK en_US
dc.for 060112 en_US
dc.personcode 0000068216 en_US
dc.personcode 0000068217 en_US
dc.personcode 920537 en_US
dc.personcode 870145 en_US
dc.personcode 0000020342 en_US
dc.personcode 0000043010 en_US
dc.percentage 40 en_US
dc.classification.name Structural Biology (incl. Macromolecular Modelling) en_US
dc.classification.type FOR-08 en_US
dc.edition en_US
dc.custom en_US
dc.date.activity en_US
dc.location.activity en_US
dc.description.keywords molecular evolution, NMR, protein structure en_US


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