TatD DNase domain containing 3 (TATDN3)

TatD DNase domain containing 3 is a magnesium-dependent exonuclease that preferentially digests single-stranded DNA and RNA from the 3′- to 5′-end, with some apurinic/apyrimidinic endonuclease activity observed in vitro[1][2]. Structurally, it contains a TIM-barrel motif, which is common in enzymes with diverse catalytic activities[1]. Functionally, TATDN3 is implicated in DNA repair processes, including nucleotide excision and double-strand break repair, and has additional suggested roles in apoptotic DNA fragmentation[1]. Its activity is essential for maintaining genome integrity, particularly in response to oxidative DNA damage. The protein is evolutionarily conserved across species, underscoring its fundamental biological importance[1][3]. Specific disease associations, drug interactions, and clinical utility remain under investigation, with most current data supporting its general relevance to DNA repair and apoptosis[1][2][3][4].

Other names

Deoxyribonuclease TATDN3DNA-(apurinic or apyrimidinic site) endonuclease TATDN3Putative deoxyribonuclease TATDN3TATDN3

Not established for specific drugs. Hypothetically, inhibitors would block exonuclease activity and interfere with DNA repair; activators could enhance genome stability.