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http://purl.uniprot.org/citations/8232218http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8232218http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/8232218http://www.w3.org/2000/01/rdf-schema#comment"A new peptide antagonist of voltage-activated calcium channels was purified from venom of the funnel web spider, Agelenopsis aperta. This 48-amino acid peptide, omega-agatoxin (omega-Aga)-IVB, was found to be a potent (Kd, approximately 3 nM) blocker of P-type calcium channels in rat cerebellar Purkinje neurons but had no activity against T-type, L-type, or N-type calcium channels in a variety of neurons. The calcium channel-blocking properties of omega-Aga-IVB were similar to those of another toxin, omega-Aga-IVA, which has 71% amino acid identity with omega-Aga-IVB. The 10-fold greater abundance of omega-Aga-IVB in venom allowed structural studies using NMR spectroscopy. The three-dimensional structure derived from NMR data resulted in a proposed disulfide bond configuration for the peptide. Although omega-Aga-IVB has fewer basic and more acidic residues than does omega-Aga-IVA, the two toxins show conservation of positively charged residues in a mid-peptide region that is predicted to form one face of the omega-Aga-IVB molecule. This region may be crucial for high affinity binding to the P-type calcium channel. In contrast, the amino termini of the two toxins have different charges and seem unlikely to be involved in binding to the channel."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Adams M.E."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Adams M.E."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Thanabal V."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Thanabal V."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Bean B.P."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Bean B.P."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Mintz I.M."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Mintz I.M."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Reily M.D."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/author"Reily M.D."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/date"1993"xsd:gYear
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/name"Mol. Pharmacol."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/name"Mol. Pharmacol."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/pages"681-688"xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/pages"681-688"xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/title"Structure and properties of omega-agatoxin IVB, a new antagonist of P-type calcium channels."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/title"Structure and properties of omega-agatoxin IVB, a new antagonist of P-type calcium channels."xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/8232218http://purl.uniprot.org/core/volume"44"xsd:string
http://purl.uniprot.org/citations/8232218http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8232218
http://purl.uniprot.org/citations/8232218http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/8232218