RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/7552747http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7552747http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7552747http://www.w3.org/2000/01/rdf-schema#comment"The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.org/dc/terms/identifier"doi:10.1038/nsb0995-758"xsd:string
http://purl.uniprot.org/citations/7552747http://purl.org/dc/terms/identifier"doi:10.1038/nsb0995-758"xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/author"Tanaka T."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/author"Tanaka T."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/author"Zhang M."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/author"Ikura M."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/author"Ikura M."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/pages"758-767"xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/pages"758-767"xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/title"Calcium-induced conformational transition revealed by the solution structure of apo calmodulin."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/title"Calcium-induced conformational transition revealed by the solution structure of apo calmodulin."xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/volume"2"xsd:string
http://purl.uniprot.org/citations/7552747http://purl.uniprot.org/core/volume"2"xsd:string
http://purl.uniprot.org/citations/7552747http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7552747
http://purl.uniprot.org/citations/7552747http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/7552747
http://purl.uniprot.org/citations/7552747http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7552747
http://purl.uniprot.org/citations/7552747http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/7552747