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Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2017,1,10]]},"abstract":"<jats:title>Significance<\/jats:title>\n                  <jats:p>\n                    This study explores the structural basis for the difference between the closely related Na\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase and H\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase with respect to ion transport stoichiometry, electrogenicity, and cation selectivity, which has long been an enigma. A cysteine in the membrane domain of Na\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase is substituted by arginine in H\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase and has been found to be replaced by phenylalanine in a patient with alternating hemiplegia of childhood. These substitutions affect the functioning of the Na\n                    <jats:sup>+<\/jats:sup>\n                    -specific site of Na\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase profoundly. The positively charged side chain of the arginine present in H\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase serves as an internal cation that replaces bound Na\n                    <jats:sup>+<\/jats:sup>\n                    , thus explaining how H\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase avoids binding and transporting Na\n                    <jats:sup>+<\/jats:sup>\n                    at this site, thereby performing electroneutral transport, despite the general structural and functional resemblance to the electrogenic Na\n                    <jats:sup>+<\/jats:sup>\n                    ,K\n                    <jats:sup>+<\/jats:sup>\n                    -ATPase.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1617951114","type":"journal-article","created":{"date-parts":[[2016,12,27]],"date-time":"2016-12-27T20:50:24Z","timestamp":1482871824000},"page":"316-321","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":19,"title":["Arginine substitution of a cysteine in transmembrane helix M8 converts Na\n                    <sup>+<\/sup>\n                    ,K\n                    <sup>+<\/sup>\n                    -ATPase to an electroneutral pump similar to H\n                    <sup>+<\/sup>\n                    ,K\n                    <sup>+<\/sup>\n                    -ATPase"],"prefix":"10.1073","volume":"114","author":[{"given":"Rikke","family":"Holm","sequence":"first","affiliation":[{"name":"Department of Biomedicine, Aarhus University, 8000 Aarhus C, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jaanki","family":"Khandelwal","sequence":"additional","affiliation":[{"name":"Department of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, Texas Tech University Health Sciences Center, Lubbock, TX 79430"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anja P.","family":"Einholm","sequence":"additional","affiliation":[{"name":"Department of Biomedicine, Aarhus University, 8000 Aarhus C, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jens P.","family":"Andersen","sequence":"additional","affiliation":[{"name":"Department of Biomedicine, Aarhus University, 8000 Aarhus C, Denmark;"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pablo","family":"Artigas","sequence":"additional","affiliation":[{"name":"Department of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, Texas Tech University Health 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