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http://purl.uniprot.org/citations/10891072http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10891072http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10891072http://www.w3.org/2000/01/rdf-schema#comment"Calcium vector protein (CaVP) from amphioxus is a two-domain, calcium-binding protein (18.3 kDa) of the calmodulin superfamily. Only two of the four EF-hand motifs (sites III and IV) have a significant binding affinity for calcium ions. We determined the solution structure of the domain containing these active sites (C-CaVP: W81-S161), in the Ca(2+)-saturated state, using NMR spectroscopy and restrained molecular dynamics. The tertiary structure is similar to other Ca(2+)-binding domains containing a pair of EF-hand motifs. The apo state has spectroscopic and thermodynamic characteristics of a molten globule, with conserved secondary structure but highly fluctuating tertiary organization. Titration of C-CaVP with Ca(2+) revealed a stepwise ion binding, with a stable equilibrium intermediate in which only site III binds a calcium ion. Despite a highly fluctuating structure of the free site IV, the calcium-bound site III has a persistent structure, with similar secondary elements but different interhelix angle and hydrophobic packing relative to the fully calcium-saturated state."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.org/dc/terms/identifier"doi:10.1021/bi000360z"xsd:string
http://purl.uniprot.org/citations/10891072http://purl.org/dc/terms/identifier"doi:10.1021/bi000360z"xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Sakamoto H."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Sakamoto H."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Cox J.A."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Cox J.A."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Craescu C.T."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Craescu C.T."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Baladi S."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Baladi S."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Theret I."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/author"Theret I."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/name"Biochemistry"xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/pages"7920-7926"xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/pages"7920-7926"xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/title"Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/title"Sequential calcium binding to the regulatory domain of calcium vector protein reveals functional asymmetry and a novel mode of structural rearrangement."xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/volume"39"xsd:string
http://purl.uniprot.org/citations/10891072http://purl.uniprot.org/core/volume"39"xsd:string