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http://purl.uniprot.org/citations/12192410http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12192410http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12192410http://www.w3.org/2000/01/rdf-schema#comment"Large-conductance (BK type) Ca(2+)-dependent K(+) channels are essential for modulating muscle contraction and neuronal activities such as synaptic transmission and hearing. BK channels are activated by membrane depolarization and intracellular Ca(2+) and Mg(2+) (refs 6-10). The energy provided by voltage, Ca(2+) and Mg(2+) binding are additive in activating the channel, suggesting that these signals open the activation gate through independent pathways. Here we report a molecular investigation of a Mg(2+)-dependent activation mechanism. Using a combined site-directed mutagenesis and structural analysis, we demonstrate that a structurally new Mg(2+)-binding site in the RCK/Rossman fold domain --an intracellular structural motif that immediately follows the activation gate S6 helix --is responsible for Mg(2+)-dependent activation. Mutations that impair or abolish Mg(2+) sensitivity do not affect Ca(2+) sensitivity, and vice versa. These results indicate distinct structural pathways for Mg(2+)- and Ca(2+)-dependent activation and suggest a possible mechanism for the coupling between Mg(2+) binding and channel opening."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.org/dc/terms/identifier"doi:10.1038/nature00941"xsd:string
http://purl.uniprot.org/citations/12192410http://purl.org/dc/terms/identifier"doi:10.1038/nature00941"xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Shi J."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Shi J."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Qin J."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Qin J."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Yang Y."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Yang Y."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Hu L."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Hu L."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Cui J."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Cui J."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Chaturvedi N."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Chaturvedi N."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Krishnamoorthy G."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Krishnamoorthy G."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Harilal D."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/author"Harilal D."xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/12192410http://purl.uniprot.org/core/name"Nature"xsd:string