d61097a9ba7ce3d3ace0f50f88ca351b cel_a2020m4v9n4p1038.pdf 5453f5508bce2c290ec60989a3e2720084296d41 cel_a2020m4v9n4p1038.pdf cca863f38067e3c0787df4d8da7876ac1a834eca05b621c3ebfe6ab2f1f6a2a6 cel_a2020m4v9n4p1038.pdf Title: Structural and Biophysical Insights into the Function of the Intrinsically Disordered Myc Oncoprotein Subject: Myc is a transcription factor driving growth and proliferation of cells and involved in the majority of human tumors. Despite a huge body of literature on this critical oncogene, our understanding of the exact molecular determinants and mechanisms that underlie its function is still surprisingly limited. Indubitably though, its crucial and non-redundant role in cancer biology makes it an attractive target. However, achieving successful clinical Myc inhibition has proven challenging so far, as this nuclear protein is an intrinsically disordered polypeptide devoid of any classical ligand binding pockets. Indeed, Myc only adopts a (partially) folded structure in some contexts and upon interacting with some protein partners, for instance when dimerizing with MAX to bind DNA. Here, we review the cumulative knowledge on Myc structure and biophysics and discuss the implications for its biological function and the development of improved Myc inhibitors. We focus this biophysical walkthrough mainly on the basic region helix–loop–helix leucine zipper motif (bHLHLZ), as it has been the principal target for inhibitory approaches so far. Keywords: Myc; MAX; protein–protein interactions; protein–DNA interactions; intrinsically disordered proteins; biophysics; drug discovery Author: Marie-Eve Beaulieu, Francisco Castillo and Laura Soucek Creator: LaTeX with hyperref package Producer: pdfTeX-1.40.18 CreationDate: Wed Apr 22 10:23:17 2020 CEST ModDate: Wed Apr 22 10:23:17 2020 CEST Tagged: no UserProperties: no Suspects: no Form: none JavaScript: no Pages: 27 Encrypted: no Page size: 595.276 x 841.89 pts (A4) Page rot: 0 File size: 2443429 bytes Optimized: no PDF version: 1.5 name type encoding emb sub uni object ID ------------------------------------ ----------------- ---------------- --- --- --- --------- TZEHRB+URWPalladioL-Ital Type 1 Custom yes yes no 94 0 RAONWZ+URWPalladioL-Bold Type 1 Custom yes yes no 95 0 YUNKBK+URWPalladioL-Roma Type 1 Custom yes yes no 96 0 WIZZQD+VnURWPalladioL Type 1 Custom yes yes no 97 0 QJKKBB+Rpxr Type 1 Builtin yes yes no 98 0 PFKOHU+TimesNewRomanPS-BoldItalicMT Type 1C WinAnsi yes yes 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