tudor domain

KDM4-IN-4 (compound 47) is a potent inhibitor of histone lysine demethylase 4 (KDM4), with a binding constant of approximately 80 μM for the KDM4A-Tudor domain. It inhibits H3K4Me3 binding to the Tudor domain in cellular contexts with an EC50 value of 105 μM, holding potential for anticancer research applications [1].

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.

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

NV03 is a potent and selective antagonist of the UHRF1 (Ubiquitin-like with PHD and RING finger domains 1)-H3K9me3 interaction, binding to the UHRF1 tandem tudor domain with a Kd of 2.4 μM. NV03 holds potential as an anticancer therapeutic [1].

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].

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].

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].

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.

WAG003 is a Tudor domain inhibitor.