KMT2A and cancer: For example, antagonistsof WDR5 can disrupt its interaction with Mixed Lineage Leukemia (MLL)histone methyltransferase (Figure S2a),thereby abrogating MLL function to suppress growth in leukemia andbreast cancer.6−9 Similarly, small molecule antagonism of the central pocket of EED(Figure S2b), a WDR subunit of the polycombrepression complex 2 (PRC2), disrupts binding of PRC2-stimulatoryproteins with concomitant inhibition of PRC2 catalytic activity.10,11