Abstract

Protein-protein interactions between members of the Myc transcription factor network are potential targets of small molecule inhibitors and stabilizers. Diverse screening strategies, including fluorescence resonance energy transfer, fluorescence polarization, two hybrid and protein complementation assays have identified several lead compounds that inhibit Myc-Max dimerization and one compound that stabilizes the Max homodimer. Representative compounds interfere with Myc-induced transcriptional activation, Myc-mediated oncogenic transformation, Myc-driven cellular replication and DNA binding of Myc. For the best characterized compounds, specific binding sites have been determined, and molecular mechanisms of action have been documented. This knowledge of small molecule - protein interaction is currently applied to highly targeted approaches that seek to identify novel compounds with improved potency.

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