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Themeasles virus nucleoprotein consists of a structured N\u2010terminal domain, and of an intrinsically disordered C\u2010terminal domain, N<jats:sub>TAIL<\/jats:sub> (aa 401\u2013525), which undergoes induced folding in the presence of the C\u2010terminal domain (XD, aa 459\u2013507) of the viral phosphoprotein. With in N<jats:sub>TAIL<\/jats:sub>, an \u03b1\u2010helical molecular recognition element (\u03b1\u2010MoRE, aa 488\u2013499) involved in binding to P and in induced folding was identified and then observed in the crystal structure of XD. Using small\u2010angle X\u2010ray scattering, we have derived a low\u2010resolution structural model of the complex between XD and N<jats:sub>TAIL<\/jats:sub>, which shows that most of N<jats:sub>TAIL<\/jats:sub> remains disordered in the complex despite P\u2010induced folding within the \u03b1\u2010MoRE. The model consists of an extended shape accommodating the multiple conformations adopted by the disordered N\u2010terminal region of N<jats:sub>TAIL<\/jats:sub>, and of a bulky globular region, corresponding to XD and to the C terminus of N<jats:sub>TAIL<\/jats:sub> (aa 486\u2013525). Using surface plasmon resonance, circular dichroism, fluorescence spectroscopy, and heteronuclear magnetic resonance, we show that N<jats:sub>TAIL<\/jats:sub> has an additional site (aa 517\u2013525) involved in binding to XD but not in the unstructured\u2010to\u2010structured transition. This work provides evidence that intrinsically disordered domains can establish complex interactions with their partners, and can contact them through multiple sites that do not all necessarily gain regular secondary structure.<\/jats:p>","DOI":"10.1110\/ps.051411805","type":"journal-article","created":{"date-parts":[[2005,7,26]],"date-time":"2005-07-26T19:57:47Z","timestamp":1122407867000},"page":"1975-1992","source":"Crossref","is-referenced-by-count":144,"title":["The intrinsically disordered C\u2010terminal domain of the measles virus nucleoprotein interacts with the C\u2010terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolded"],"prefix":"10.1002","volume":"14","author":[{"given":"Jean\u2010Marie","family":"Bourhis","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"V\u00e9ronique","family":"Receveur\u2010Br\u00e9chot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael","family":"Oglesbee","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xinsheng","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Matthew","family":"Buccellato","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Herv\u00e9","family":"Darbon","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bruno","family":"Canard","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"St\u00e9phanie","family":"Finet","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sonia","family":"Longhi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2009,1]]},"reference":[{"key":"e_1_2_7_2_1","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1996.0060"},{"key":"e_1_2_7_3_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0021889800008372"},{"key":"e_1_2_7_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0965-1748(01)00171-0"},{"key":"e_1_2_7_5_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi015763t"},{"key":"e_1_2_7_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.virusres.2003.11.007"},{"key":"e_1_2_7_7_1","first-page":"730","article-title":"Immunoaffinity purification of FLAG epitope\u2010tagged bacterial alkaline phosphatase using a novel monoclonal antibody and peptide elution","volume":"16","author":"Brizzard B.L.","year":"1994","journal-title":"Biotechniques"},{"key":"e_1_2_7_8_1","doi-asserted-by":"publisher","DOI":"10.1128\/jvi.67.10.5803-5812.1993"},{"key":"e_1_2_7_9_1","doi-asserted-by":"publisher","DOI":"10.1099\/0022-1317-70-2-435"},{"key":"e_1_2_7_10_1","doi-asserted-by":"publisher","DOI":"10.1128\/JVI.75.3.1117-1123.2001"},{"key":"e_1_2_7_11_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi047817f"},{"key":"e_1_2_7_12_1","doi-asserted-by":"publisher","DOI":"10.1006\/viro.1996.0359"},{"key":"e_1_2_7_13_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0065-3527(08)60373-5"},{"key":"e_1_2_7_14_1","doi-asserted-by":"crossref","first-page":"4358","DOI":"10.1128\/jvi.67.7.4358-4364.1993","article-title":"The hypervariable C\u2010terminal tail of the Sendai paramyxovirus nucleocapsid protein is required for template function but not for RNA encapsidation","volume":"67","author":"Curran J.","year":"1993","journal-title":"J. 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