Regulation of MYC-MAX DNA binding in cancer.Part 2: The MYC-MAX heterodimer
The MYC protein is a central hub in cellular growth control and a key regulator of gene expression. To bind DNA, the c-terminal region of MYC must form a heterodimer with the protein MAX. Our recent proteomic mapping of the MYC interactome using mass spectrometry suggests that the conserved MYC regions MBIIIb and MBIV functionally collaborate with the bHLHZ region in regulating tumorigenicity. Crystal and NMR structures of MYC-MAX have to date only included the core DNA-binding bHLHzip rmotif, thus structural contributions by flanking regions remain unknown. As a first step towards investigating the full MYC-MAX-DNA assembly we have studied MAX-MAX-DNA by SANS, where our data suggest that flanking MAX regions co-fold with its bHLHZ both alone and on DNA. We now aim to investigate the DNA-bound MYC-MAX heterodimer, including regulatory regions N-terminal to the MYC bHLHZ region. By strategic deuteration we aim to derive the separate structured envelopes of MYC and MAX to elucidate the degree of co-folding. Better understanding of the MYC-MAX structure will significantly enhance development of cancer therapeutics targeting this complex as well as its regulatory interactors.
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The recommended format for citing this dataset in a research publication is in the following format:
Francesca Caporaletti; MARTEL Anne; MOPARTHI Vamsi Krishna; PIETRAS Zuzanna; SUNNERHAGEN Maria and WALLNER Bjorn. (2020). Regulation of MYC-MAX DNA binding in cancer.Part 2: The MYC-MAX heterodimer. Institut Laue-Langevin (ILL) doi:10.5291/ILL-DATA.8-03-1003
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This data is not yet public
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