| http://purl.uniprot.org/citations/15583008 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15583008 | http://www.w3.org/2000/01/rdf-schema#comment | "The Na(+)/Ca(2+)-K(+) exchanger (NCKX) extrudes Ca(2+) from cells utilizing both the inward Na(+) gradient and the outward K(+) gradient. NCKX is thought to operate by a consecutive mechanism in which a cation binding pocket accommodates both Ca(2+) and K(+) and alternates between inward and outward facing conformations. Here we developed a simple fluorometric method to analyze changes in K(+) and Ca(2+) dependences of mutant NCKX2 proteins in which candidate residues within membrane-spanning domains were substituted. The largest shifts in both K(+) and Ca(2+) dependences compared with wild-type NCKX2 were observed for the charge-conservative substitutions of Glu(188) and Asp(548), whereas the size-conservative substitutions resulted in nonfunctional proteins. Substitution of several other residues including two proline residues (Pro(187) and Pro(547)), three additional acidic residues (Asp(258), Glu(265), Glu(533)), and two hydroxyl-containing residues (Ser(185) and Ser(545)) showed smaller shifts, but shifts in Ca(2+) dependence were invariably accompanied by shifts in K(+) dependence. We conclude that Glu(188) and Asp(548) are the central residues of a single cation binding pocket that can accommodate both K(+) and Ca(2+). Furthermore, a single set of residues lines a transport pathway for both K(+) and Ca(2+)."xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m407933200"xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/author | "Kinjo T.G."xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/author | "Kang K.J."xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/author | "Schnetkamp P.P."xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/author | "Szerencsei R.T."xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/date | "2005"xsd:gYear |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/pages | "6823-6833"xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/title | "Residues contributing to the Ca2+ and K+ binding pocket of the NCKX2 Na+/Ca2+-K+ exchanger."xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://purl.uniprot.org/core/volume | "280"xsd:string |
| http://purl.uniprot.org/citations/15583008 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/15583008 |
| http://purl.uniprot.org/citations/15583008 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/15583008 |
| http://purl.uniprot.org/uniprot/#_Q9UI40-mappedCitation-15583008 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/15583008 |
| http://purl.uniprot.org/uniprot/Q9UI40 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/15583008 |