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http://purl.uniprot.org/citations/9708977http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9708977http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9708977http://www.w3.org/2000/01/rdf-schema#comment"Conotoxins are valuable probes of receptors and ion channels because of their small size and highly selective activity. alpha-Conotoxin EpI, a 16-residue peptide from the mollusk-hunting Conus episcopatus, has the amino acid sequence GCCSDPRCNMNNPDY(SO3H)C-NH2 and appears to be an extremely potent and selective inhibitor of the alpha3beta2 and alpha3beta4 neuronal subtypes of the nicotinic acetylcholine receptor (nAChR). The desulfated form of EpI ([Tyr15]EpI) has a potency and selectivity for the nAChR receptor similar to those of EpI. Here we describe the crystal structure of [Tyr15]EpI solved at a resolution of 1.1 A using SnB. The asymmetric unit has a total of 284 non-hydrogen atoms, making this one of the largest structures solved de novo by direct methods. The [Tyr15]EpI structure brings to six the number of alpha-conotoxin structures that have been determined to date. Four of these, [Tyr15]EpI, PnIA, PnIB, and MII, have an alpha4/7 cysteine framework and are selective for the neuronal subtype of the nAChR. The structure of [Tyr15]EpI has the same backbone fold as the other alpha4/7-conotoxin structures, supporting the notion that this conotoxin cysteine framework and spacing give rise to a conserved fold. The surface charge distribution of [Tyr15]EpI is similar to that of PnIA and PnIB but is likely to be different from that of MII, suggesting that [Tyr15]EpI and MII may have different binding modes for the same receptor subtype."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.org/dc/terms/identifier"doi:10.1021/bi9806549"xsd:string
http://purl.uniprot.org/citations/9708977http://purl.org/dc/terms/identifier"doi:10.1021/bi9806549"xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Alewood P.F."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Alewood P.F."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Lewis R.J."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Lewis R.J."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Martin J.L."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Martin J.L."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Miller R."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Miller R."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Hu S.H."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Hu S.H."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Blessing R.H."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Blessing R.H."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Loughnan M."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Loughnan M."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Weeks C.M."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/author"Weeks C.M."xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/9708977http://purl.uniprot.org/core/name"Biochemistry"xsd:string