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http://purl.uniprot.org/citations/19580749http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/19580749http://www.w3.org/2000/01/rdf-schema#comment"Voltage-gated K+ channels share a common voltage sensor domain (VSD) consisting of four transmembrane helices, including a highly mobile S4 helix that contains the major gating charges. Activation of ether-a-go-go (EAG) family K+ channels is sensitive to external divalent cations. We show here that divalent cations slow the activation rate of two EAG family channels (Kv12.1 and Kv10.2) by forming a bridge between a residue in the S4 helix and acidic residues in S2. Histidine 328 in the S4 of Kv12.1 favors binding of Zn2+ and Cd2+, whereas the homologous residue Serine 321 in Kv10.2 contributes to effects of Mg2+ and Ni2+. This novel finding provides structural constraints for the position of transmembrane VSD helices in closed, ion-bound EAG family channels. Homology models of Kv12.1 and Kv10.2 VSD structures based on a closed-state model of the Shaker family K+ channel Kv1.2 match these constraints. Our results suggest close conformational conservation between closed EAG and Shaker family channels, despite large differences in voltage sensitivity, activation rates, and activation thresholds."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.org/dc/terms/identifier"doi:10.1016/j.bpj.2009.04.032"xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/author"Chen B."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/author"Lee C.C."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/author"Jegla T."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/author"Bursulaya B."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/author"Pivaroff K."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/date"2009"xsd:gYear
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/name"Biophys J"xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/pages"110-120"xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/title"Divalent cations slow activation of EAG family K+ channels through direct binding to S4."xsd:string
http://purl.uniprot.org/citations/19580749http://purl.uniprot.org/core/volume"97"xsd:string
http://purl.uniprot.org/citations/19580749http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/19580749
http://purl.uniprot.org/citations/19580749http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/19580749
http://purl.uniprot.org/uniprot/#_A1L3C4-mappedCitation-19580749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/#_F6TUN6-mappedCitation-19580749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/#_P59111-mappedCitation-19580749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/#_Q8BLY4-mappedCitation-19580749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/#_Q920E3-mappedCitation-19580749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/#_Q6NZH0-mappedCitation-19580749http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/Q6NZH0http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/A1L3C4http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19580749
http://purl.uniprot.org/uniprot/F6TUN6http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/19580749