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http://purl.uniprot.org/citations/10467092http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10467092http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10467092http://www.w3.org/2000/01/rdf-schema#comment"The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.org/dc/terms/identifier"doi:10.1038/12271"xsd:string
http://purl.uniprot.org/citations/10467092http://purl.org/dc/terms/identifier"doi:10.1038/12271"xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Furuya T."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Furuya T."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Ikura M."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Ikura M."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Kurihara H."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Kurihara H."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Osawa M."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Osawa M."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Tokumitsu H."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Tokumitsu H."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Swindells M.B."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Swindells M.B."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Orita M."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Orita M."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Shibanuma T."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/author"Shibanuma T."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string
http://purl.uniprot.org/citations/10467092http://purl.uniprot.org/core/name"Nat. Struct. Biol."xsd:string