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Exonuclease 3'-5' domain-containing protein 2 (EXD2) is an enzyme belonging to the DEDDy superfamily of 3'-5' exonucleases, with a unique dimeric structure found on the mitochondrial outer membrane[1][5]. EXD2 exhibits both 3'-5' exonuclease and exoribonuclease activities, participating in the processing of DNA double-strand breaks (DSBs) for homologous recombination repair and in the degradation of RNA, particularly within RNA–DNA hybrids[3][6]. Structural and biochemical analyses indicate substrate discrimination based on metal ion coordination and a preference for RNA over DNA in hybrid duplexes[6]. EXD2 is essential for the recovery of transcription following genotoxic stress and contributes to the maintenance of genome stability[7]. Current evidence suggests it is a multifaceted molecule with roles in nuclear DNA repair and mitochondrial function, although the full range of its in vivo activities remains under investigation[4][5][6][7]. No drugs directly targeting this enzyme are yet described in the literature.
No clinically validated drugs directly targeting EXD2 are reported; mechanisms would likely involve inhibition or modulation of exonuclease activity, affecting DNA repair or mitochondrial function
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