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Fig. 1 | Journal of Hematology & Oncology

Fig. 1

From: Structure, function and inhibition of critical protein–protein interactions involving mixed lineage leukemia 1 and its fusion oncoproteins

Fig. 1

MLL1 and oncogenic MLL1 fusion proteins. a Illustrations of MLL1 and onco-MLL1 fusion proteins showing their functional domains. MLL1 with 3969 amino acids contains domains of (from the N- to C-terminus) Menin-binding motif (MBM, residues 2–40), LEDGF-binding domain (LBD, 109–153), AT-hooks (ATHs, 142–400), nuclear-localization signals 1 and 2 (SNL1, 400–443 and SNL2, 1008–1106), CxxC domain (1147–1337), plant homology domains 1–4 (PHD1, 1431–1482; PHD2, 1479–1533; PHD3, 1566–1627; PHD4, 1931–1978), bromodomain (BRD, 1703–1748), FYRN domain (2018–2074), Taspase 1 cleavage sites 1 and 2 (TCS1, 2666–2670 and TCS2, 2718–2722), transactivation domain (TAD, 2829–2883), FYRC domain (3666–3747), WDR5 interaction motif (Win, 3762–3773), and SET domain (3829–2945). The breakpoints of MLL1 are located in the region of ~ 1400. b Frequencies of the MLL1 fusion partner proteins in the clinic, with transcription cofactors AF4 (36%), AF9 (19%) and its paralog ENL (13%), AF10 (8%), ELL (4%) and AF6 (4%) being the most common. c Illustration of current approaches to inhibit PPIs involving MLL1 and its fusion proteins

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