Please use this identifier to cite or link to this item: https://doi.org/10.1096/fj.08-113555
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dc.titleIrditoxin, a novel covalently linked heterodimeric three-finger toxin with high taxon-specific neurotoxicity
dc.contributor.authorPawlak, J.
dc.contributor.authorMackessy, S.P.
dc.contributor.authorSixberry, N.M.
dc.contributor.authorStura, E.A.
dc.contributor.authorLe Du, M.H.
dc.contributor.authorMéenez, R.
dc.contributor.authorFoo, C.S.
dc.contributor.authorMénez, A.
dc.contributor.authorNirthanan, S.
dc.contributor.authorKini, R.M.
dc.date.accessioned2014-10-27T08:32:08Z
dc.date.available2014-10-27T08:32:08Z
dc.date.issued2009-02
dc.identifier.citationPawlak, J., Mackessy, S.P., Sixberry, N.M., Stura, E.A., Le Du, M.H., Méenez, R., Foo, C.S., Ménez, A., Nirthanan, S., Kini, R.M. (2009-02). Irditoxin, a novel covalently linked heterodimeric three-finger toxin with high taxon-specific neurotoxicity. FASEB Journal 23 (2) : 534-545. ScholarBank@NUS Repository. https://doi.org/10.1096/fj.08-113555
dc.identifier.issn08926638
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100974
dc.description.abstractA novel heterodimeric three-finger neurotoxin, irditoxin, was isolated from venom of the brown treesnake Boiga irregularis (Colubridae). Irditoxin subunit amino acid sequences were determined by Edman degradation and cDNA sequencing. The crystal structure revealed two subunits with a three-finger protein fold, typical for "nonconventional" toxins such as denmotoxin, bucandin, and candoxin. This is the first colubrid three- finger toxin dimer, covalently connected via an interchain disulfide bond. Irditoxin showed taxon-specific lethality toward birds and lizards and was nontoxic toward mice. It produced a potent neuromuscular blockade at the avian neuromuscular junction (IC 50=10 nM), comparable to α-bungarotoxin, but was three orders of magnitude less effective at the mammalian neuromuscular junction. Co- valently linked heterodimeric three-finger toxins found in colubrid venoms constitute a new class of venom pep- tides, which may be a useful source of new neurobiology probes and therapeutic leads. © FASEB.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1096/fj.08-113555
dc.sourceScopus
dc.subjectAcetylcholine receptor
dc.subjectNeuromuscular junction
dc.subjectPostsynaptic neurotoxin
dc.subjectSnake venom
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1096/fj.08-113555
dc.description.sourcetitleFASEB Journal
dc.description.volume23
dc.description.issue2
dc.description.page534-545
dc.description.codenFAJOE
dc.identifier.isiut000262892900025
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