{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,6,10]],"date-time":"2026-06-10T16:44:51Z","timestamp":1781109891382,"version":"3.54.1"},"reference-count":33,"publisher":"National Academy of Sciences","issue":"6","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2008,2,12]]},"abstract":"<jats:p>\n                    Ectromelia virus (ECTV) encodes an IFN-\u03b3-binding protein (IFN-\u03b3BP\n                    <jats:sup>ECTV<\/jats:sup>\n                    ) that disrupts IFN-\u03b3 signaling and its ability to induce an antiviral state within cells. IFN-\u03b3BP\n                    <jats:sup>ECTV<\/jats:sup>\n                    is an important virulence factor that is highly conserved (&gt;90%) in all orthopoxviruses, including variola virus, the causative agent of smallpox. The 2.2-\u212b crystal structure of the IFN-\u03b3BP\n                    <jats:sup>ECTV<\/jats:sup>\n                    \/IFN-\u03b3 complex reveals IFN-\u03b3BP\n                    <jats:sup>ECTV<\/jats:sup>\n                    consists of an IFN-\u03b3R1 ligand-binding domain and a 57-aa helix-turn-helix (HTH) motif that is structurally related to the transcription factor TFIIA. The HTH motif forms a tetramerization domain that results in an IFN-\u03b3BP\n                    <jats:sup>ECTV<\/jats:sup>\n                    \/IFN-\u03b3 complex containing four IFN-\u03b3BP\n                    <jats:sup>ECTV<\/jats:sup>\n                    chains and two IFN-\u03b3 dimers. The structure, combined with biochemical and cell-based assays, demonstrates that IFN-\u03b3BP\n                    <jats:sup>ECTV<\/jats:sup>\n                    tetramers are required for efficient IFN-\u03b3 antagonism.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0705753105","type":"journal-article","created":{"date-parts":[[2008,2,5]],"date-time":"2008-02-05T21:09:03Z","timestamp":1202245743000},"page":"1861-1866","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":32,"title":["Structure and mechanism of IFN-\u03b3 antagonism by an orthopoxvirus IFN-\u03b3-binding protein"],"prefix":"10.1073","volume":"105","author":[{"given":"Anthony A.","family":"Nuara","sequence":"first","affiliation":[{"name":"*Center for Biophysical Sciences and Engineering and"},{"name":"Department of Molecular Microbiology and Immunology, Saint Louis University Health Sciences Center, St. Louis, MO 63104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Leigh J.","family":"Walter","sequence":"additional","affiliation":[{"name":"*Center for Biophysical Sciences and Engineering and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Naomi J.","family":"Logsdon","sequence":"additional","affiliation":[{"name":"*Center for Biophysical Sciences and Engineering and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sung Il","family":"Yoon","sequence":"additional","affiliation":[{"name":"*Center for Biophysical Sciences and Engineering and"},{"name":"Department of Microbiology, University of Alabama at Birmingham, Birmingham, AL 35294; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brandi C.","family":"Jones","sequence":"additional","affiliation":[{"name":"*Center for Biophysical Sciences and Engineering and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jill M.","family":"Schriewer","sequence":"additional","affiliation":[{"name":"Department of Molecular Microbiology and Immunology, Saint Louis University Health Sciences Center, St. Louis, MO 63104"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"R. 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