{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,5]],"date-time":"2026-10-05T04:06:06Z","timestamp":1791173166951,"version":"4.1.0"},"reference-count":43,"publisher":"National Academy of Sciences","issue":"11","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2010,3,16]]},"abstract":"<jats:p>\n                    ORAI1 is the pore-forming subunit of the calcium release-activated calcium (CRAC) channel, a store-operated channel that is central to Ca\n                    <jats:sup>2+<\/jats:sup>\n                    signaling in mammalian cells. Electrophysiological data have shown that the acidic residues E106 in transmembrane helix 1 (TM1) and E190 in TM3 contribute to the high selectivity of ORAI1 channels for Ca\n                    <jats:sup>2+<\/jats:sup>\n                    . We have examined the pore architecture of the ORAI1 channel using ORAI1 proteins engineered to contain either one or two cysteine residues. Disulfide cross-linking shows that ORAI1 assembles as a tetramer or a higher oligomer with TM1 centrally located. Cysteine side chains projecting from TM1 at position 88, 95, 102, or 106 cross-link efficiently to the corresponding side chain in a second ORAI1 monomer. Cysteine residues at position 190 or at surrounding positions in TM3 do not cross-link. We conclude that E106 residues in wild-type ORAI1 are positioned to form a Ca\n                    <jats:sup>2+<\/jats:sup>\n                    binding site in the channel pore and that E190 interacts less directly with ions traversing the pore. The cross-linking data further identify a relatively rigid segment of TM1 adjacent to E106 that is likely to contribute to the selectivity filter.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1001169107","type":"journal-article","created":{"date-parts":[[2010,3,1]],"date-time":"2010-03-01T23:55:41Z","timestamp":1267487741000},"page":"4896-4901","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":140,"title":["Pore architecture of the ORAI1 store-operated calcium channel"],"prefix":"10.1073","volume":"107","author":[{"given":"Yubin","family":"Zhou","sequence":"first","affiliation":[{"name":"Immune Disease Institute and Program in Cellular and Molecular Medicine, Children\u2019s Hospital Boston, 200 Longwood Avenue, Boston, MA 02115; and"},{"name":"Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sweta","family":"Ramachandran","sequence":"additional","affiliation":[{"name":"Immune Disease Institute and Program in Cellular and Molecular Medicine, Children\u2019s Hospital Boston, 200 Longwood Avenue, Boston, MA 02115; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masatsugu","family":"Oh-hora","sequence":"additional","affiliation":[{"name":"Immune Disease Institute and Program in Cellular and Molecular Medicine, Children\u2019s Hospital Boston, 200 Longwood Avenue, Boston, MA 02115; and"},{"name":"Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anjana","family":"Rao","sequence":"additional","affiliation":[{"name":"Immune Disease Institute and Program in Cellular and Molecular Medicine, Children\u2019s Hospital Boston, 200 Longwood Avenue, Boston, MA 02115; and"},{"name":"Department of Pathology, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Patrick G.","family":"Hogan","sequence":"additional","affiliation":[{"name":"Immune Disease Institute and Program in Cellular and Molecular Medicine, Children\u2019s Hospital Boston, 200 Longwood Avenue, Boston, MA 02115; 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