Tudor domain-containing protein 3 (TDRD3)

Tudor domain-containing protein 3 (TDRD3) is a multidomain scaffold and adaptor protein characterized by the presence of a Tudor domain that binds to arginine-methylated motifs in proteins, in addition to an OB-fold, a ubiquitin-associated (UBA) domain, and DUF1767. TDRD3 primarily localizes in the cytoplasm, where it plays critical roles in the regulation of transcription and translation, stress granule dynamics, and the assembly of post-transcriptional regulatory complexes. It forms a complex with topoisomerase 3β (Top3β), modulating both DNA and RNA topoisomerase activities, and is implicated in epigenetic reading on chromatin. Its overexpression is associated with poor prognosis in certain cancers (notably estrogen receptor-negative breast cancer) and may contribute to neurodevelopmental and psychiatric conditions. The Tudor domain is being explored as a target for small molecule antagonists aiming to disrupt disease-related protein interactions[1][2][3][4].

Other names

FLJ21007tudor domain containing 3TDRD3

Small molecule antagonists block the methyl-binding surface of the Tudor domain, disrupting protein-protein interactions relevant to chromatin engagement and post-transcriptional regulation[3]