{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T03:19:42Z","timestamp":1791083982124,"version":"4.1.0"},"reference-count":61,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"28","content-domain":{"domain":["www.science.org"],"crossmark-restriction":true},"short-container-title":["Sci. Adv."],"published-print":{"date-parts":[[2025,7,11]]},"abstract":"<jats:p>\n            Coronavirus envelope (E) proteins form drug-targeted ion channels that cause virulence to infected cells. The Middle East respiratory syndrome (MERS) virus has high mortality rates, but its E structure and function are unknown. We report the single-channel conductance and structure of membrane-bound MERS E protein. MERS E conducts K\n            <jats:sup>+<\/jats:sup>\n            ions with a unitary conductance of 113 picosiemens, fivefold larger than the conductance of severe acute respiratory syndrome coronavirus 2 E. Solid-state nuclear magnetic resonance data indicate that the MERS E transmembrane domain forms a five-helix bundle that spans the lipid bilayer. The amino-terminal helical interface features multiple interacting phenylalanine (Phe) residues and an asparagine (Asn), whereas the carboxyl-terminal channel pore contains Phe\n            <jats:sup>33<\/jats:sup>\n            . Mutation of Phe\n            <jats:sup>17<\/jats:sup>\n            abolished K\n            <jats:sup>+<\/jats:sup>\n            conductance, whereas mutations of Phe\n            <jats:sup>33<\/jats:sup>\n            and Asn\n            <jats:sup>15<\/jats:sup>\n            suppressed most channel activity. These results indicate that MERS E contains two Phe-centered ion-conduction apparatuses, which likely permeate ions through cation-\u03c0 interactions, providing the structural basis for developing antiviral drugs to inhibit this pathogenic viroporin.\n          <\/jats:p>","DOI":"10.1126\/sciadv.adx1788","type":"journal-article","created":{"date-parts":[[2025,7,9]],"date-time":"2025-07-09T17:58:57Z","timestamp":1752083937000},"update-policy":"https:\/\/doi.org\/10.34133\/aaas_crossmark","source":"Crossref","is-referenced-by-count":14,"title":["Ion channel structure and function of the MERS coronavirus E protein"],"prefix":"10.1126","volume":"11","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-1192-7800","authenticated-orcid":true,"given":"Iva","family":"Su\u010dec","sequence":"first","affiliation":[{"name":"Department of Chemistry, Massachusetts Institute of Technology, 170 Albany Street, Cambridge, MA 02139, 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