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http://purl.uniprot.org/citations/15150794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15150794http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15150794http://www.w3.org/2000/01/rdf-schema#comment"The solution structure of contryphan-Vn, a cyclic peptide with a double cysteine S-S bridge and containing a D-tryptophan extracted from the venom of the cone snail Conus ventricosus, has been determined by NMR spectroscopy using a variety of homonuclear and heteronuclear NMR methods and restrained molecular dynamics simulations. The main conformational features of backbone contryphan-Vn are a type IV beta-turn from Gly 1 to Lys 6 and a type I beta-turn from Lys 6 to Cys 9. As already found in other contryphans, one of the two prolines--the Pro4--is mainly in the cis conformation while Pro7 is trans. A small hydrophobic region probably partly shielded from solvent constituted from the close proximity of side chains of Pro7 and Trp8 was observed together with a persistent salt bridge between Asp2 and Lys6, which has been revealed by the diagnostic observation of specific nuclear Overhauser effects. The salt bridge was used as a restraint in the molecular dynamics in vacuum but without inserting explicit electrostatic contribution in the calculations. The backbone of the unique conformational family found of contryphan-Vn superimposes well with those of contryphan-Sm and contryphan-R. This result indicates that the contryphan structural motif represents a robust and conserved molecular scaffold whose main structural determinants are the size of the intercysteine loop and the presence and location in the sequence of the D-Trp and the two Pro residues."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.org/dc/terms/identifier"doi:10.1002/bip.20025"xsd:string
http://purl.uniprot.org/citations/15150794http://purl.org/dc/terms/identifier"doi:10.1002/bip.20025"xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Polticelli F."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Polticelli F."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Ascenzi P."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Ascenzi P."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Schinina M.E."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Schinina M.E."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Cicero D.O."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Cicero D.O."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Paci M."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Paci M."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Eliseo T."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Eliseo T."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Massilia G.R."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Massilia G.R."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Romeo C."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/author"Romeo C."xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/name"Biopolymers"xsd:string
http://purl.uniprot.org/citations/15150794http://purl.uniprot.org/core/name"Biopolymers"xsd:string