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http://purl.uniprot.org/citations/17142296http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17142296http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/17142296http://www.w3.org/2000/01/rdf-schema#comment"Mu-conotoxins are three-loop peptides produced by cone snails to inhibit voltage-gated sodium channels during prey capture. Using polymerase chain reaction techniques, we identified a gene sequence from the venom duct of Conus tulipa encoding a new mu-conotoxin-TIIIA (TIIIA). A 125I-TIIIA binding assay was established to isolate native TIIIA from the crude venom of Conus striatus. The isolated peptide had three post-translational modifications, including two hydroxyproline residues and C-terminal amidation, and <35% homology to other mu-conotoxins. TIIIA potently displaced [3H]saxitoxin and 125I-TIIIA from rat brain (Nav1.2) and skeletal muscle (Nav1.4) membranes. Alanine and glutamine scans of TIIIA revealed several residues, including Arg14, that were critical for high-affinity binding to tetrodotoxin (TTX)-sensitive Na+ channels. We were surprised to find that [E15A]TIIIA had a 10-fold higher affinity than TIIIA for TTX-sensitive sodium channels (IC50, 15 vs. 148 pM at rat brain membrane). TIIIA was selective for Nav1.2 and -1.4 over Nav1.3, -1.5, -1.7, and -1.8 expressed in Xenopus laevis oocytes and had no effect on rat dorsal root ganglion neuron Na+ current. 1H NMR studies revealed that TIIIA adopted a single conformation in solution that was similar to the major conformation described previously for mu-conotoxin PIIIA. TIIIA and analogs provide new biochemical probes as well as insights into the structure-activity of mu-conotoxins."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.org/dc/terms/identifier"doi:10.1124/mol.106.028225"xsd:string
http://purl.uniprot.org/citations/17142296http://purl.org/dc/terms/identifier"doi:10.1124/mol.106.028225"xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Adams D.J."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Adams D.J."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Alewood P.F."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Alewood P.F."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Lewis R.J."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Lewis R.J."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Schroeder C.I."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Schroeder C.I."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Thomas L."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Thomas L."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Nielsen K.J."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Nielsen K.J."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Adams D.A."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Adams D.A."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Drinkwater R."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Drinkwater R."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Loughnan M."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Loughnan M."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Ekberg J."xsd:string
http://purl.uniprot.org/citations/17142296http://purl.uniprot.org/core/author"Ekberg J."xsd:string