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The structure showed how the S1\u2013S4 domain and its associated linker can serve as a clamp to constrain the gate of the pore and possibly function in concert with ligand-binding domains to regulate the opening of the pore. The structure also led us to hypothesize a new mechanism by which motions of the S6 inner helices can gate the ion conduction pathway at a position along the pore closer to the selectivity filter than the canonical helix bundle crossing.<\/jats:p>","DOI":"10.1073\/pnas.0711533105","type":"journal-article","created":{"date-parts":[[2008,1,23]],"date-time":"2008-01-23T21:00:17Z","timestamp":1201122017000},"page":"1511-1515","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":146,"title":["Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel"],"prefix":"10.1073","volume":"105","author":[{"given":"Gina M.","family":"Clayton","sequence":"first","affiliation":[{"name":"Department of Molecular Biophysics and Biochemistry, Yale University, 260 Whitney Avenue, New Haven, CT 06520"}]},{"given":"Steve","family":"Altieri","sequence":"additional","affiliation":[{"name":"Department of Molecular Biophysics and 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