Regulation of Myc-Max DNA binding in cancer: The Max homodimer
The Myc-Max heterodimer assembly functions as a central hub in cellular growth control, by regulating a wealth of biological functions including proliferation, apoptosis, differentiation, and transformation. Uncontrolled Myc expression disturbs the carefully tuned balance of cell growth regulation, which turns the Myc-Max heterodimer into an oncoprotein multimodular platform and a key contributor to the development of many human cancers. To bind DNA, the c-terminal region of Myc must form a heterodimer with the protein Max. Crystal structures describing the Myc-Max and Max-Max dimers have so far only included the core DNA-binding motif, including the bHLHzip region. By circular dichroism spectroscopy, we have shown that regions flanking the Max bHLHzip core add significant helical propensity, which does not agree with a bHLHzip core flanked by disordered regions. Furthermore, we found that the full-length Max-Max homodimer is more stable than the Max-bHLHzip homodimer. Here, we will use SANS to describe the full Max-Max-DNA envelope. Neutron scattering envelopes in this project will be critical to proceed towards modelling of the full Myc-Max-DNA heterodimer structures.
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Francesca Caporaletti; GABEL Frank; MARTEL Anne; PIETRAS Zuzanna; SUNNERHAGEN Maria and WALLNER Bjorn. (2019). Regulation of Myc-Max DNA binding in cancer: The Max homodimer. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-05-442
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