Insights into the mechanism of Apoptin's exquisitely selective anti-tumor action from atomic level characterization of its conformation and dynamics

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• 作者：Santiago Ruiz-Martí ; nez^a ; David Pantoja-Uceda^b ; Jessica Castro^a ; Maria Vilanova^a ; Marc Ribó ; ^a ; Marta Bruix^b ; Antoni Benito^a ; ^{antoni.benito@udg.edu} ; Douglas V. Laurents^b ; ^{dlaurents@iqfr.csic.es}
• 关键词：Anti-cancer protein ; Phosphorylation ; Intrinsically disordered protein ; NMR spectroscopy
• 刊名：Archives of Biochemistry and Biophysics
• 出版年：2017
• 出版时间：15 January 2017
• 年：2017
• 卷：614
• 期：Complete
• 页码：53-64
• 全文大小：2827 K
• 卷排序：614

文摘

Apoptin is an anti-cancer protein from chicken anemia virus. WT Apoptin is oligomeric and hard to characterize. Here, we have characterized, at atomic level, a soluble, active monomeric Apoptin variant. This variant is intrinsically disordered and its specific phosphorylation does not induce folding. These results have relevance for understanding WT Apoptin's mechanism of action.