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http://purl.uniprot.org/citations/21402935http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21402935http://www.w3.org/2000/01/rdf-schema#comment"Structures of the prokaryotic K(+) channel, KcsA, highlight the role of the selectivity filter carbonyls from the GYG signature sequence in determining a highly selective pore, but channels displaying this sequence vary widely in their cation selectivity. Furthermore, variable selectivity can be found within the same channel during a process called C-type inactivation. We investigated the mechanism for changes in selectivity associated with inactivation in a model K(+) channel, KcsA. We found that E71A, a noninactivating KcsA mutant in which a hydrogen-bond behind the selectivity filter is disrupted, also displays decreased K(+) selectivity. In E71A channels, Na(+) permeates at higher rates as seen with and flux measurements and analysis of intracellular Na(+) block. Crystal structures of E71A reveal that the selectivity filter no longer assumes the "collapsed," presumed inactivated, conformation in low K(+), but a "flipped" conformation, that is also observed in high K(+), high Na(+), and even Na(+) only conditions. The data reveal the importance of the E71-D80 interaction in both favoring inactivation and maintaining high K(+) selectivity. We propose a molecular mechanism by which inactivation and K(+) selectivity are linked, a mechanism that may also be at work in other channels containing the canonical GYG signature sequence."xsd:string
http://purl.uniprot.org/citations/21402935http://purl.org/dc/terms/identifier"doi:10.1073/pnas.1014186108"xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/author"McCoy J.G."xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/author"Nichols C.G."xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/author"Cheng W.W."xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/author"Nimigean C.M."xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/author"Thompson A.N."xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/name"Proc Natl Acad Sci U S A"xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/pages"5272-5277"xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/title"Mechanism for selectivity-inactivation coupling in KcsA potassium channels."xsd:string
http://purl.uniprot.org/citations/21402935http://purl.uniprot.org/core/volume"108"xsd:string
http://purl.uniprot.org/citations/21402935http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/21402935
http://purl.uniprot.org/citations/21402935http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/21402935
http://purl.uniprot.org/uniprot/P0A334#attribution-E905682C67D572846CC39A4BF2B2C018http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/21402935
http://purl.uniprot.org/uniprot/#_P0A334-mappedCitation-21402935http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/21402935
http://purl.uniprot.org/uniprot/P0A334http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/21402935