| http://purl.uniprot.org/citations/20508092 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20508092 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/20508092 | http://www.w3.org/2000/01/rdf-schema#comment | "High-conductance voltage- and Ca2+-activated K+ (BK) channels encode negative feedback regulation of membrane voltage and Ca2+ signaling, playing a central role in numerous physiological processes. We determined the x-ray structure of the human BK Ca2+ gating apparatus at a resolution of 3.0 angstroms and deduced its tetrameric assembly by solving a 6 angstrom resolution structure of a Na+-activated homolog. Two tandem C-terminal regulator of K+ conductance (RCK) domains from each of four channel subunits form a 350-kilodalton gating ring at the intracellular membrane surface. A sequence of aspartic amino acids that is known as the Ca2+ bowl, and is located within the second of the tandem RCK domains, creates four Ca2+ binding sites on the outer perimeter of the gating ring at the "assembly interface" between RCK domains. Functionally important mutations cluster near the Ca2+ bowl, near the "flexible interface" between RCK domains, and on the surface of the gating ring that faces the voltage sensors. The structure suggests that the Ca2+ gating ring, in addition to regulating the pore directly, may also modulate the voltage sensor."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1190414"xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.org/dc/terms/identifier | "doi:10.1126/science.1190414"xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "MacKinnon R."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "MacKinnon R."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Yuan P."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Yuan P."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Hsiung Y."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Hsiung Y."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Leonetti M.D."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Leonetti M.D."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Pico A.R."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/author | "Pico A.R."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/date | "2010"xsd:gYear |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/name | "Science"xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/pages | "182-186"xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/pages | "182-186"xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/title | "Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/title | "Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution."xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/volume | "329"xsd:string |
| http://purl.uniprot.org/citations/20508092 | http://purl.uniprot.org/core/volume | "329"xsd:string |