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- W2046246154 abstract "The transcription factor c-MYC is an intrinsically disordered oncoprotein that undergoes coupled folding and binding to its obligate dimerization partner MAX. Upon dimerization c-MYC and MAX form a basic helix-loop-helix leucine zipper conformation. Many forms of cancer have been associated with the overexpression of c-MYC. Previously we have identified three independent small molecule binding sites on c-MYC that stabilize the disordered, monomeric form and inhibit dimerization with MAX. One of these small molecule inhibitors, 10074-G5, binds specifically to a short amino acid sequence in helix 1 of the monomeric c-MYC. Each amino acid in this binding region was individually changed to an alanine residue in order to investigate the binding contributions for each amino acid of the site. Substituting the amino acids of the binding site for alanine may also alter the conformation of the inhibitor binding site, innately changing the c-MYC affinity for 10074-G5. Using this method to analyze the direct and indirect amino acid contributions to 10074-G5 binding will not only provide further insight into defining the functional epitope of the 10074-G5 binding site of c-MYC, but also provide insight to the conformational requirements to maintain or enhance inhibitor affinity." @default.
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- W2046246154 date "2011-02-01" @default.
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- W2046246154 title "Alanine Scan of a Small Molecule Interaction Site on the Disordered c-Myc Oncoprotein" @default.
- W2046246154 doi "https://doi.org/10.1016/j.bpj.2010.12.532" @default.
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