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http://purl.uniprot.org/citations/12860384http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12860384http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12860384http://www.w3.org/2000/01/rdf-schema#comment"Six peptide toxins (Magi 1-6) were isolated from the Hexathelidae spider Macrothele gigas. The amino acid sequences of Magi 1, 2, 5 and 6 have low similarities to the amino acid sequences of known spider toxins. The primary structure of Magi 3 is similar to the structure of the palmitoylated peptide named PlTx-II from the North American spider Plectreurys tristis (Plectreuridae). Moreover, the amino acid sequence of Magi 4, which was revealed by cloning of its cDNA, displays similarities to the Na+ channel modifier delta-atracotoxin from the Australian spider Atrax robustus (Hexathelidae). Competitive binding assays using several 125I-labelled peptide toxins clearly demonstrated the specific binding affinity of Magi 1-5 to site 3 of the insect sodium channel and also that of Magi 5 to site 4 of the rat sodium channel. Only Magi 6 did not compete with the scorpion toxin LqhalphaIT in binding to site 3 despite high toxicity on lepidoptera larvae of 3.1 nmol/g. The K(i)s of other toxins were between 50 pM for Magi 4 and 1747 nM for Magi 1. In addition, only Magi 5 binds to both site 3 in insects (K(i)=267 nM) and site 4 in rat brain synaptosomes (K(i)=1.2 nM), whereas it showed no affinities for either mammal binding site 3 or insect binding site 4. Magi 5 is the first spider toxin with binding affinity to site 4 of a mammalian sodium channel."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(03)00666-5"xsd:string
http://purl.uniprot.org/citations/12860384http://purl.org/dc/terms/identifier"doi:10.1016/s0014-5793(03)00666-5"xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Dai L."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Dai L."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Gilles N."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Gilles N."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Nakajima T."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Nakajima T."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Satake H."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Satake H."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Corzo G."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Corzo G."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Haupt J."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Haupt J."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Villegas E."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/author"Villegas E."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/date"2003"xsd:gYear
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/name"FEBS Lett."xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/pages"43-50"xsd:string
http://purl.uniprot.org/citations/12860384http://purl.uniprot.org/core/pages"43-50"xsd:string