{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,8]],"date-time":"2026-09-08T12:58:18Z","timestamp":1788872298734,"version":"build-2803163510"},"reference-count":27,"publisher":"Wiley","issue":"7","license":[{"start":{"date-parts":[[2014,5,9]],"date-time":"2014-05-09T00:00:00Z","timestamp":1399593600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"name":"Italian Ministero dell'Istruzione dell'Universit\u00e0 e della Ricerca"},{"DOI":"10.13039\/501100004271","name":"Sapienza University of Rome","doi-asserted-by":"crossref","award":["C26A13T9NB"],"award-info":[{"award-number":["C26A13T9NB"]}],"id":[{"id":"10.13039\/501100004271","id-type":"DOI","asserted-by":"crossref"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Protein Science"],"published-print":{"date-parts":[[2014,7]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>The KIX domain is a mediator of the interaction between different transcription factors. This complex function is carried out via two distinct binding sites located on opposite sides of the protein; namely, the \u2018c\u2010Myb site\u2019 and the \u2018MLL site\u2019, named after their characteristic ligands\u2014the transactivation domain of c\u2010Myb and the mixed lineage leukemia protein (MLL). Both these ligands are unstructured in isolation and fold only upon binding, posing the KIX domain as an ideal candidate to explore the binding induced folding reaction of intrinsically unstructured proteins. Here, we complement the recent kinetic description on the interaction between KIX and c\u2010Myb, by characterizing the binding kinetics between KIX and MLL, at different pH and ionic strength conditions. Furthermore, we analyze quantitatively the mechanism of allosteric communication between the topologically distinct c\u2010Myb and MLL sites. The implications of our results are discussed in the light of previous work on other intrinsically unstructured systems.<\/jats:p>","DOI":"10.1002\/pro.2480","type":"journal-article","created":{"date-parts":[[2014,4,19]],"date-time":"2014-04-19T07:22:18Z","timestamp":1397892138000},"page":"962-969","source":"Crossref","is-referenced-by-count":39,"title":["The mechanism of binding of the KIX domain to the mixed lineage leukemia protein and its allosteric role in the recognition of c\u2010Myb"],"prefix":"10.1002","volume":"23","author":[{"given":"Angelo","family":"Toto","sequence":"first","affiliation":[{"name":"Istituto Pasteur\u2014Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR Dipartimento di Scienze Biochimiche \u201cA. Rossi Fanelli\u201d Sapienza Universit\u00e0 di Roma 00185 Rome Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rajanish","family":"Giri","sequence":"additional","affiliation":[{"name":"Istituto Pasteur\u2014Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR Dipartimento di Scienze Biochimiche \u201cA. Rossi Fanelli\u201d Sapienza Universit\u00e0 di Roma 00185 Rome Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maurizio","family":"Brunori","sequence":"additional","affiliation":[{"name":"Istituto Pasteur\u2014Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR Dipartimento di Scienze Biochimiche \u201cA. Rossi Fanelli\u201d Sapienza Universit\u00e0 di Roma 00185 Rome Italy"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stefano","family":"Gianni","sequence":"additional","affiliation":[{"name":"Istituto Pasteur\u2014Fondazione Cenci Bolognetti and Istituto di Biologia e Patologia Molecolari del CNR Dipartimento di Scienze Biochimiche \u201cA. Rossi Fanelli\u201d Sapienza Universit\u00e0 di Roma 00185 Rome Italy"},{"name":"Department of Chemistry University of Cambridge Lensfield Road Cambridge CB2 1EW UK"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2014,5,9]]},"reference":[{"key":"e_1_2_6_2_1","doi-asserted-by":"publisher","DOI":"10.1038\/386569a0"},{"key":"e_1_2_6_3_1","doi-asserted-by":"publisher","DOI":"10.1101\/gad.14.13.1553"},{"key":"e_1_2_6_4_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.tibs.2005.03.011"},{"key":"e_1_2_6_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80463-8"},{"key":"e_1_2_6_6_1","article-title":"Molecular recognition by the KIX domain and its role in gene regulation","author":"Thakur JK","year":"2013","journal-title":"Nucleic Acids Res"},{"key":"e_1_2_6_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2005.09.059"},{"key":"e_1_2_6_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M207660200"},{"key":"e_1_2_6_9_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.jmb.2004.01.038"},{"key":"e_1_2_6_10_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbrc.2012.09.112"},{"key":"e_1_2_6_11_1","doi-asserted-by":"publisher","DOI":"10.1016\/0022-2836(92)90561-W"},{"key":"e_1_2_6_12_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1307337110"},{"key":"e_1_2_6_13_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.90.16.7884"},{"key":"e_1_2_6_14_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.22.10610"},{"key":"e_1_2_6_15_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja809947w"},{"key":"e_1_2_6_16_1","doi-asserted-by":"publisher","DOI":"10.1021\/cb4002188"},{"key":"e_1_2_6_17_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.1313548110"},{"key":"e_1_2_6_18_1","volume-title":"Hemoglobin and myoglobin in their reactions with ligands","author":"Antonini E","year":"1971"},{"key":"e_1_2_6_19_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2005.03.072"},{"key":"e_1_2_6_20_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.sbi.2008.10.002"},{"key":"e_1_2_6_21_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.bbapap.2010.01.017"},{"key":"e_1_2_6_22_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja803221c"},{"key":"e_1_2_6_23_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M112.399436"},{"key":"e_1_2_6_24_1","doi-asserted-by":"publisher","DOI":"10.1021\/ja309527h"},{"key":"e_1_2_6_25_1","doi-asserted-by":"publisher","DOI":"10.1039\/c3cp54226b"},{"key":"e_1_2_6_26_1","doi-asserted-by":"publisher","DOI":"10.1021\/cb900190u"},{"key":"e_1_2_6_27_1","doi-asserted-by":"publisher","DOI":"10.1021\/bi802055v"},{"key":"e_1_2_6_28_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0022-2836(65)80285-6"}],"container-title":["Protein Science"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fpro.2480","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1002%2Fpro.2480","content-type":"unspecified","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1002\/pro.2480","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,15]],"date-time":"2023-09-15T19:25:17Z","timestamp":1694805917000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1002\/pro.2480"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,5,9]]},"references-count":27,"journal-issue":{"issue":"7","published-print":{"date-parts":[[2014,7]]}},"alternative-id":["10.1002\/pro.2480"],"URL":"https:\/\/doi.org\/10.1002\/pro.2480","archive":["Portico"],"relation":{},"ISSN":["0961-8368","1469-896X"],"issn-type":[{"value":"0961-8368","type":"print"},{"value":"1469-896X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2014,5,9]]}}}