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, JJ
dc.contributor.author Hill, JM
dc.contributor.author Little, MJ
dc.contributor.author Nicholson, GM
dc.contributor.author King, GF
dc.contributor.author Alewood, PF
dc.date.accessioned 2012-10-12T03:33:24Z
dc.date.issued 2011-06-28
dc.identifier.citation Proceedings of the National Academy of Sciences of the United States of America, 2011, 108 (26), pp. 10478 - 10483
dc.identifier.issn 0027-8424
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 β-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.
dc.language eng
dc.relation.hasversion Accepted manuscript version en_US
dc.relation.isbasedon 10.1073/pnas.1103501108
dc.title Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif
dc.type Journal Article
dc.description.version Published
dc.parent Proceedings of the National Academy of Sciences of the United States of America
dc.journal.volume 26
dc.journal.volume 108
dc.journal.number 26 en_US
dc.publocation Washington, DC USA en_US
dc.publocation Perth, Australia
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.conference ANZMAC
dc.for 060112 Structural Biology (Incl. Macromolecular Modelling)
dc.for 030406 Proteins and Peptides
dc.personcode 920537
dc.personcode 870145
dc.percentage 50 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.date.activity 2011-11-28
dc.location.activity en_US
dc.location.activity Perth, Australia
dc.description.keywords Molecular evolution
dc.description.keywords NMR
dc.description.keywords Protein structure
pubs.embargo.period Not known
pubs.organisational-group /University of Technology Sydney
pubs.organisational-group /University of Technology Sydney/Faculty of Science
pubs.organisational-group /University of Technology Sydney/Strength - Health Technologies
utslib.copyright.status Open Access
utslib.copyright.date 2015-04-15 12:23:47.074767+10
pubs.consider-herdc true
utslib.collection.history Uncategorised (ID: 363)
utslib.collection.history General (ID: 2)


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