RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/16478480http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16478480http://www.w3.org/2000/01/rdf-schema#comment"Human ether à go-go potassium channels (hEAG1) open in response to membrane depolarization and they are inhibited by Ca2+/calmodulin (CaM), presumably binding to the C-terminal domain of the channel subunits. Deletion of the cytosolic N-terminal domain resulted in complete abolition of Ca2+/CaM sensitivity suggesting the existence of further CaM binding sites. A peptide array-based screen of the entire cytosolic protein of hEAG1 identified three putative CaM-binding domains, two in the C-terminus (BD-C1: 674-683, BD-C2: 711-721) and one in the N-terminus (BD-N: 151-165). Binding of GST-fusion proteins to Ca2+/CaM was assayed with fluorescence correlation spectroscopy, surface plasmon resonance spectroscopy and precipitation assays. In the presence of Ca2+, BD-N and BD-C2 provided dissociation constants in the nanomolar range, BD-C1 bound with lower affinity. Mutations in the binding domains reduced inhibition of the functional channels by Ca2+/CaM. Employment of CaM-EF-hand mutants showed that CaM binding to the N- and C-terminus are primarily dependent on EF-hand motifs 3 and 4. Hence, closure of EAG channels presumably requires the binding of multiple CaM molecules in a manner more complex than previously assumed."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.org/dc/terms/identifier"doi:10.1111/j.1742-4658.2006.05134.x"xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Heinemann S.H."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Schonherr R."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Kullertz G."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Malesevic M."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Born A.K."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Gavrilova-Ruch O."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Glaser R.W."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/author"Ziechner U."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/date"2006"xsd:gYear
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/name"FEBS J"xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/pages"1074-1086"xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/title"Inhibition of human ether a go-go potassium channels by Ca2+/calmodulin binding to the cytosolic N- and C-termini."xsd:string
http://purl.uniprot.org/citations/16478480http://purl.uniprot.org/core/volume"273"xsd:string
http://purl.uniprot.org/citations/16478480http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/16478480
http://purl.uniprot.org/citations/16478480http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/16478480
http://purl.uniprot.org/uniprot/#_A0A0S1TJ81-mappedCitation-16478480http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16478480
http://purl.uniprot.org/uniprot/#_A0A0S1TL27-mappedCitation-16478480http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16478480
http://purl.uniprot.org/uniprot/#_A0A977NV57-mappedCitation-16478480http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16478480
http://purl.uniprot.org/uniprot/#_O95259-mappedCitation-16478480http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16478480
http://purl.uniprot.org/uniprot/#_L8EAS2-mappedCitation-16478480http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/16478480
http://purl.uniprot.org/uniprot/A0A0S1TL27http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16478480
http://purl.uniprot.org/uniprot/L8EAS2http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/16478480