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http://purl.uniprot.org/citations/12149279http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12149279http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/12149279http://www.w3.org/2000/01/rdf-schema#comment"We report here a combination of site-directed mutations that eliminate the high-affinity Ca(2+) response of the large-conductance Ca(2+)-activated K(+) channel (BK(Ca)), leaving only a low-affinity response blocked by high concentrations of Mg(2+). Mutations at two sites are required, the "Ca(2+) bowl," which has been implicated previously in Ca(2+) binding, and M513, at the end of the channel's seventh hydrophobic segment. Energetic analyses of mutations at these positions, alone and in combination, argue that the BK(Ca) channel contains three types of Ca(2+) binding sites, one of low affinity that is Mg(2+) sensitive (as has been suggested previously) and two of higher affinity that have similar binding characteristics and contribute approximately equally to the power of Ca(2+) to influence channel opening. Estimates of the binding characteristics of the BK(Ca) channel's high-affinity Ca(2+)-binding sites are provided."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.org/dc/terms/identifier"doi:10.1085/jgp.20028627"xsd:string
http://purl.uniprot.org/citations/12149279http://purl.org/dc/terms/identifier"doi:10.1085/jgp.20028627"xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Bao L."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Bao L."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Cox D.H."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Cox D.H."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Holmstrand E.C."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Holmstrand E.C."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Rapin A.M."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/author"Rapin A.M."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/date"2002"xsd:gYear
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/name"J. Gen. Physiol."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/name"J. Gen. Physiol."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/pages"173-189"xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/pages"173-189"xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/title"Elimination of the BK(Ca) channel's high-affinity Ca(2+) sensitivity."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/title"Elimination of the BK(Ca) channel's high-affinity Ca(2+) sensitivity."xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/volume"120"xsd:string
http://purl.uniprot.org/citations/12149279http://purl.uniprot.org/core/volume"120"xsd:string
http://purl.uniprot.org/citations/12149279http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12149279
http://purl.uniprot.org/citations/12149279http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/12149279