UNC3474, a small molecule ligand, selectively interacts with the aromatic methyl-lysine binding cage of the tumor protein 53BP1 Tudor domain (TT), exhibiting a dissociation constant (Kd) of 1.0±0.3 μM. It impedes 53BP1's recruitment to DNA double-strand breaks (DSBs), maintaining the protein's autoinhibited state within cells [1].

UNC926 (UNC-926) inhibits L3MBTL1 (IC50: 3.9 μM). UNC926 also exhibits a low micromolar affinity for L3MBTL3. UNC926 inhibits binding of the 3xMBT domain to H4K20me1. It selectively and dose-dependently inhibits the L3MBTL13xMBT-H4K20me1 interaction. UNC926 has not an effect on the binding of 53BP1 to H4K20me1.

Tumor protein p53 binding protein (53BP1) has been identified in a yeast two-hybrid screen as a protein that interacts with the central DNA–binding domain of p532. Similar to breast cancer susceptibility gene 13, 4 (BRCA1; 53BP1 enhances p53-dependent tra

UNC9512 is a potent antagonist of the methyl-lysine reader protein 53BP1, which can be utilized to investigate the function of 53BP1 in DNA repair, gene editing, and tumorigenesis [1].

53BP1-binding protein 1 (53BP1) engages with dimethylated lysine 20 on histone 4 (H4K20me2) through its tandem tudor domains within a homodimer configuration, crucial for the DNA damage response. UNC2170, a micromolar 53BP1 ligand, selectively interacts with this site, demonstrating at least 17-fold preference for 53BP1 over similar proteins. This interaction occurs in a pocket formed by the 53BP1's tudor domains. Moreover, UNC2170 acts as an antagonist to 53BP1 in cellular lysates, effectively inhibiting class switch recombination, a process dependent on the functional 53BP1 tudor domain, thus confirming its cellular activity.

UNC-2170 (UNC2170 Maleate) is the methyl-lysine binding protein, 53BP1 ligand.