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http://purl.uniprot.org/citations/11517232http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11517232http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11517232http://www.w3.org/2000/01/rdf-schema#comment"The auxiliary beta-subunit KCNMB2 (beta(2)) endows the non-inactivating large conductance Ca(2+)- and voltage-dependent potassium (BK) channel with fast inactivation. This process is mediated by the N terminus of KCNMB2 and closely resembles the "ball-and-chain"-type inactivation observed in voltage-gated potassium channels. Here we investigated the solution structure and function of the KCNMB2 N terminus (amino acids 1-45, BKbeta(2)N) using NMR spectroscopy and patch clamp recordings. BKbeta(2)N completely inactivated BK channels when applied to the cytoplasmic side; its interaction with the BK alpha-subunit is characterized by a particularly slow dissociation rate and an affinity in the upper nanomolar range. The BKbeta(2)N structure comprises two domains connected by a flexible linker: the pore-blocking "ball domain" (formed by residues 1-17) and the "chain domain" (between residues 20-45) linking it to the membrane segment of KCNMB2. The ball domain is made up of a flexible N terminus anchored at a well ordered loop-helix motif. The chain domain consists of a 4-turn helix with an unfolded linker at its C terminus. These structural properties explain the functional characteristics of BKbeta(2)N-mediated inactivation."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m107118200"xsd:string
http://purl.uniprot.org/citations/11517232http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m107118200"xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Bentrop D."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Bentrop D."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Beyermann M."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Beyermann M."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Fakler B."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Fakler B."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Wissmann R."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/author"Wissmann R."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/date"2001"xsd:gYear
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/pages"42116-42121"xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/pages"42116-42121"xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/title"NMR structure of the 'ball-and-chain' domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/title"NMR structure of the 'ball-and-chain' domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels."xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11517232http://purl.uniprot.org/core/volume"276"xsd:string
http://purl.uniprot.org/citations/11517232http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11517232
http://purl.uniprot.org/citations/11517232http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11517232