tudor domain

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

KDM4-IN-4 is a histone lysine demethylase 4 (KDM4) inhibitor that primarily targets the Tudor domain of KDM4A and exhibits anticancer activity. KDM4-IN-4 has an affinity for the KDM4A Tudor domain of approximately 80 μM. KDM4-IN-4 inhibits the binding of H3K4Me3 to the Tudor domain in cells, with an EC50 of 105 μM. KDM4-IN-4 can be used in cancer research.

SETDB1-TTD-IN-1 is a potent and selective inhibitor of SET domain bifurcated protein 1 tandem tudor domain (SETDB1-TTD, Kd = 88 nM), and also an endogenous binder competitive inhibitor with a KD of 0.106±0.002 μM for TTD. It can be used to study the biological functions and disease associations of SETDB1-TTD.

NV03 is a selective antagonist of the UHRF1-H3K9me3 interaction (Kd=2.4 μM), binding to the UHRF1 tandem Tudor domain (TTD) to form a complex. It is suitable for cancer research. NV03 also functions as a ligand for E3 ligases in PROTAC synthesis.

UNC6535 is a potent and reversible ligand for the SETDB1 tri-Tudor domain (3TD), with an IC50 value of 3.4 µM. It simultaneously occupies the TD2 and TD3 reader binding sites. UNC6535 exhibits weak inhibitory effects on SETDB1 methyltransferase activity, with an IC50 of 84 µM for the full-length protein. Additionally, UNC6535 shows a lack of selectivity for the 3TD and may also interact with the SET domain.

UNC7242 is an antagonist that binds to the Tudor domains of PHF1 and PHF19, with a Kd of 1.13 μM for PHF1 and 0.64 μM for PHF19. UNC7242 fails to displace full-length PHF1 or PHF19 from H3K36me3 nucleosomes or chromatin. UNC7242 is utilized in epigenetics research involving chromatin reader domain function, histone mark recognition, and polycomb-associated transcriptional regulation in malignancy-related biological systems.

UNC6535 TFA is a covalent ligand for the SETDB1 triple Tudor domain (3TD). It is capable of reversibly binding to the aromatic cages of TD2 and TD3 within SETDB1 3TD, demonstrating a weak inhibitory effect on SETDB1 methyltransferase activity, and can also displace the H3K9Me2K14Ac peptide from SETDB1 3TD.

WAG003 is a Tudor domain inhibitor.

Thymidine 3',5'-diphosphate tetrasodium (Deoxythymidine 3′,5′-diphosphate tetrasodium) acts as a selective inhibitor targeting staphylococcal nuclease, tudor domain-containing 1 (SND1, a MicroRNA regulatory complex RISC subunit), and [3,5-2H2] tyrosyl nuclease. It possesses anti-tumor properties and serves as a catalyst in various biochemical reactions [1] [2].

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].

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.

SGF29-IN-1 (Compound Cpd_DC60) serves as a selective inhibitor targeting the Tudor domain of the Spt-Ada-Gcn5 acetyltransferase (SAGA)-associated factor 29 (SGF29). It has demonstrated effectiveness in treating leukemia [1].