| http://purl.uniprot.org/citations/23831469 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/23831469 | http://www.w3.org/2000/01/rdf-schema#comment | "The BK channel, a tetrameric potassium channel with very high conductance, has a central role in numerous physiological functions. The BK channel can be activated by intracellular Ca(2+) and Mg(2+), as well as by membrane depolarization. Unlike other tetrameric potassium channels, the BK channel has seven transmembrane helices (S0-S6) including an extra helix S0. The intracellular segment between S0 and S1 (BK-IS1) is essential to BK channel functions and Asp99 in BK-IS1 is reported to be responsible for Mg(2+) coordination. In this study, BK-IS1 (44-113) was over-expressed using a bacterial system and purified in the presence of detergent micelles for multidimensional heteronuclear nuclear magnetic resonance (NMR) structural studies. Backbone resonance assignment and secondary structure analysis showed that BK-IS1 contains two amphipathic helices connected by a 36-residue loop. Amide (1)H-(15)N heteronuclear NOE analysis indicated that the loop is very flexible, while the two amphipathic helices are possibly stabilized through interaction with the membrane. A solution NMR-based titration assay of BK-IS1 was performed with various concentrations of Mg(2+). Two residues (Thr45 and Leu46) with chemical shift changes were observed but no, or very minor, chemical shift difference was observed for Asp99, indicating a possible site for binding divalent ions or other modulation partners."xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.bbrc.2013.06.091"xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/author | "Li D."xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/author | "Zhang L."xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/author | "Tian C."xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/author | "Lai C."xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/author | "Shi P."xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/date | "2013"xsd:gYear |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/name | "Biochem Biophys Res Commun"xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/pages | "408-412"xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/title | "Intracellular segment between transmembrane helices S0 and S1 of BK channel alpha subunit contains two amphipathic helices connected by a flexible loop."xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://purl.uniprot.org/core/volume | "437"xsd:string |
| http://purl.uniprot.org/citations/23831469 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/23831469 |
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