{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Zubcevic L"],"funding":["NHLBI NIH HHS","Wellcome Trust","Biotechnology and Biological Sciences Research Council"],"pagination":["15305"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4607889"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["5"],"pubmed_abstract":["Potassium channels exhibit a modular design with distinct structural and functional domains; in particular, a highly conserved pore-loop sequence that determines their ionic selectivity. We now report the functional characterisation of a novel group of functionally non-selective members of the prokaryotic 'inward rectifier' subfamily of K(+) channels. These channels share all the key structural domains of eukaryotic and prokaryotic Kir/KirBac channels, but instead possess unique pore-loop selectivity filter sequences unrelated to any other known ionic selectivity filter. The strikingly unusual architecture of these 'NirBac' channels defines a new family of functionally non-selective ion channels, and also provides important insights into the modular design of ion channels, as well as the evolution of ionic selectivity within this superfamily of tetrameric cation channels."],"journal":["Scientific reports"],"pubmed_title":["Modular Design of the Selectivity Filter Pore Loop in a Novel Family of Prokaryotic 'Inward Rectifier' (NirBac) channels."],"pmcid":["PMC4607889"],"funding_grant_id":["R01 HL054171","BB/F013035/1"],"pubmed_authors":["Nichols CG","Tucker SJ","Lee SJ","Wang S","Bavro VN","Zubcevic L"],"additional_accession":[]},"is_claimable":false,"name":"Modular Design of the Selectivity Filter Pore Loop in a Novel Family of Prokaryotic 'Inward Rectifier' (NirBac) channels.","description":"Potassium channels exhibit a modular design with distinct structural and functional domains; in particular, a highly conserved pore-loop sequence that determines their ionic selectivity. We now report the functional characterisation of a novel group of functionally non-selective members of the prokaryotic 'inward rectifier' subfamily of K(+) channels. These channels share all the key structural domains of eukaryotic and prokaryotic Kir/KirBac channels, but instead possess unique pore-loop selectivity filter sequences unrelated to any other known ionic selectivity filter. The strikingly unusual architecture of these 'NirBac' channels defines a new family of functionally non-selective ion channels, and also provides important insights into the modular design of ion channels, as well as the evolution of ionic selectivity within this superfamily of tetrameric cation channels.","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Oct","modification":"2025-04-04T13:25:09.75Z","creation":"2019-03-27T02:00:10Z"},"accession":"S-EPMC4607889","cross_references":{"pubmed":["26470642"],"doi":["10.1038/srep15305"]}}