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http://purl.uniprot.org/citations/10373375http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10373375http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10373375http://www.w3.org/2000/01/rdf-schema#comment"The omega-conotoxins are a set of structurally related, four-loop, six cysteine containing peptides, that have a range of selectivities for different subtypes of the voltage-sensitive calcium channel (VSCC). To investigate the basis of the selectivity displayed by these peptides, we have studied the binding affinities of two naturally occurring omega-conotoxins, MVIIA and MVIIC and a series of 14 MVIIA/MVIIC loop hybrids using radioligand binding assays for N and P/Q-type Ca2+channels in rat brain tissue. A selectivity profile was developed from the ratio of relative potencies at N-type VSCCs (using [125I]GVIA radioligand binding assays) and P/Q-type VSCCs (using [125I]MVIIC radioligand binding assays). In these peptides, loops 2 and 4 make the greatest contribution to VSCC subtype selectivity, while the effects of loops 1 and 3 are negligible. Peptides with homogenous combinations of loop 2 and 4 display clear selectivity preferences, while those with heterogeneous combinations of loops 2 and 4 are less discriminatory. 1H NMR spectroscopy revealed that the global folds of MVIIA, MVIIC and the 14 loop hybrid peptides were similar; however, several differences in local structure were identified. Based on the binding data and the 3D structures of MVIIA, GVIA and MVIIC, we have developed a preliminary pharmacophore based on the omega-conotoxin residues most likely to interact with the N-type VSCC."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1999.2817"xsd:string
http://purl.uniprot.org/citations/10373375http://purl.org/dc/terms/identifier"doi:10.1006/jmbi.1999.2817"xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Alewood P.F."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Alewood P.F."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Lewis R.J."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Lewis R.J."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Craik D.J."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Craik D.J."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Thomas L."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Thomas L."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Nielsen K.J."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Nielsen K.J."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Adams D."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Adams D."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Bond T."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/author"Bond T."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/name"J. Mol. Biol."xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/pages"1405-1421"xsd:string
http://purl.uniprot.org/citations/10373375http://purl.uniprot.org/core/pages"1405-1421"xsd:string