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http://purl.uniprot.org/citations/31444298http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/31444298http://www.w3.org/2000/01/rdf-schema#comment"Voltage-dependent potassium channels (Kvs) gate in response to changes in electrical membrane potential by coupling a voltage-sensing module with a K+-selective pore. Animal toxins targeting Kvs are classified as pore blockers, which physically plug the ion conduction pathway, or as gating modifiers, which disrupt voltage sensor movements. A third group of toxins blocks K+ conduction by an unknown mechanism via binding to the channel turrets. Here, we show that Conkunitzin-S1 (Cs1), a peptide toxin isolated from cone snail venom, binds at the turrets of Kv1.2 and targets a network of hydrogen bonds that govern water access to the peripheral cavities that surround the central pore. The resulting ectopic water flow triggers an asymmetric collapse of the pore by a process resembling that of inherent slow inactivation. Pore modulation by animal toxins exposes the peripheral cavity of K+ channels as a novel pharmacological target and provides a rational framework for drug design."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1908903116"xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Dym O."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Frolow F."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Gordon D."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Panyi G."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Karbat I."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Gurevitz M."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Reuveny E."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Hamer-Rogotner S."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Szanto T."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Fine S."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/author"Altman-Gueta H."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/date"2019"xsd:gYear
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/pages"18700-18709"xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/title"Pore-modulating toxins exploit inherent slow inactivation to block K+ channels."xsd:string
http://purl.uniprot.org/citations/31444298http://purl.uniprot.org/core/volume"116"xsd:string
http://purl.uniprot.org/citations/31444298http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/31444298
http://purl.uniprot.org/citations/31444298http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/31444298
http://purl.uniprot.org/uniprot/#_P0C1X2-mappedCitation-31444298http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31444298
http://purl.uniprot.org/uniprot/#_B7Z0Z2-mappedCitation-31444298http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31444298
http://purl.uniprot.org/uniprot/#_M9MSE4-mappedCitation-31444298http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31444298
http://purl.uniprot.org/uniprot/#_M9MSE6-mappedCitation-31444298http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/31444298