{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,2,21]],"date-time":"2025-02-21T12:41:21Z","timestamp":1740141681963,"version":"3.37.3"},"reference-count":39,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2014,12,12]],"date-time":"2014-12-12T00:00:00Z","timestamp":1418342400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["EY-12682"],"award-info":[{"award-number":["EY-12682"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["febs.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The FEBS Journal"],"published-print":{"date-parts":[[2015,2]]},"abstract":"<jats:p>Uncoordinated 119 protein (<jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119) is a partner of transducin\u2010\u03b1 subunit (G\u03b1<jats:sub>t<\/jats:sub>) that is essential for transducin trafficking in rod photoreceptors. The interaction is known to involve binding of the acylated N terminus of G\u03b1<jats:sub>t<\/jats:sub> to the hydrophobic pocket of <jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119. To gain insights into the mechanism of transducin trafficking, we isolated a highly pure protein complex between myristoylated chimeric G\u03b1<jats:sub>t<\/jats:sub> (G\u03b1<jats:sub>t<\/jats:sub>*) and <jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119<jats:sub>50\u2013240<\/jats:sub>, and examined the solution structure by small angle X\u2010ray scattering and chemical crosslinking. The solution structure of the G\u03b1<jats:sub>t<\/jats:sub>\u2013<jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119<jats:sub>50\u2013240<\/jats:sub> complex was derived with rigid body\/<jats:italic>ab\u00a0initio<\/jats:italic> modeling against the small angle X\u2010ray scattering data by use of known atomic structures of G\u03b1<jats:sub>t<\/jats:sub> and <jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119, and a distance constraint based on the protein crosslinking with <jats:italic>p<\/jats:italic>\u2010phenyldimaleimide. The model of the G\u03b1<jats:sub>t<\/jats:sub>\u2013<jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119<jats:sub>50\u2013240<\/jats:sub> complex indicates rotation and bending of the N\u2010terminal \u03b1\u2010helix of G\u03b1<jats:sub>t<\/jats:sub> from its position in the structure of the heterotrimeric G\u2010protein transducin (G<jats:sub>t<\/jats:sub>). This allows a\u00a0considerably more compact complex conformation, which also suggests a novel interface involving the switch <jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>\/\u03b13\u2013\u03b25 surface of G\u03b1<jats:sub>t<\/jats:sub>. Supporting a novel interface, <jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119 was found to bind full\u2010length G\u03b1<jats:sub>t<\/jats:sub>* more strongly than the G\u03b1<jats:sub>t<\/jats:sub> N\u2010terminal peptide. Furthermore, <jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119 competed with the effector molecule phosphodiesterase\u20106 \u03b3\u2010subunit, which is known to bind to the same surface of G\u03b1<jats:sub>t<\/jats:sub>. The solution structure of the G\u03b1<jats:sub>t<\/jats:sub>\u2013<jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119 complex suggests that the ability of <jats:styled-content style=\"fixed-case\">UNC<\/jats:styled-content>119 to dissociate G<jats:sub>t<\/jats:sub> subunits and release G\u03b1<jats:sub>t<\/jats:sub> from the membrane is attributable to disruption and sterical occlusion of the G\u03b2<jats:sub>1<\/jats:sub>\u03b3<jats:sub>1<\/jats:sub>\u2010binding sites on G\u03b1<jats:sub>t<\/jats:sub>.<\/jats:p>","DOI":"10.1111\/febs.13161","type":"journal-article","created":{"date-parts":[[2014,11,25]],"date-time":"2014-11-25T14:32:30Z","timestamp":1416925950000},"page":"550-561","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":3,"title":["The solution structure of the transducin\u2010\u03b1\u2013uncoordinated 119 protein complex suggests occlusion of the G\u03b2<sub>1<\/sub>\u03b3<sub>1<\/sub>\u2010binding sites"],"prefix":"10.1111","volume":"282","author":[{"given":"Pallavi","family":"Cheguru","sequence":"first","affiliation":[{"name":"Department of Molecular Physiology and Biophysics University of Iowa IA USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anurima","family":"Majumder","sequence":"additional","affiliation":[{"name":"Department of Molecular Physiology and Biophysics University of Iowa IA USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ravi","family":"Yadav","sequence":"additional","affiliation":[{"name":"Department of Molecular Physiology and Biophysics University of Iowa IA USA"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Kota N.","family":"Gopalakrishna","sequence":"additional","affiliation":[{"name":"Department of Molecular Physiology and Biophysics University of Iowa IA 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