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RUNX1/ETO, the product of the t(8;21) chromosomal translocation, is required for the onset and maintenance of one of the most common forms of acute myeloid leukemia (AML). RUNX1/ETO has a modular structure and, besides the DNA-binding domain (Runt), contains four evolutionary conserved functional domains named nervy homology regions 1-4 (NHR1 to NHR4). The NHR domains serve as docking sites for a variety of different proteins and, in addition, the NHR2 domain mediates tetramerization through hydrophobic and ionic/polar interactions. Tetramerization is essential for RUNX1/ETO oncogenic activity. Destabilization of the RUNX1/ETO high molecular weight complex abrogates RUNX1/ETO oncogenic activity. Using structure-based virtual screening, we identified several small molecule inhibitors mimicking the tetramerization hot spot within

Suppression of RUNX1/ETO oncogenic activity by a small molecule inhibitor of tetramerization