Target intelligence / Profile preview

Exonuclease 3'-5' domain-containing protein 2 (EXD2)

Target
EXD2
Molecular classification
Enzyme, Exonuclease, Nuclease (DnaQ/DEDDy family)
01

Overview

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.

Other names
EXD2C14orf114EXDL2FLJ107383'-5' exoribonuclease EXD2exonuclease 3'-5' domain-like-containing protein 2exonuclease 3'-5' domain-like 2
02

Mechanism of action

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

03

Biological functions

DNA double-strand break repairHomologous recombinationRNA degradation (exoribonuclease activity)Regulation of mitochondrial translationMaintenance of genomic stabilityTranscriptional recovery after genotoxic stress
04

Disease associations

CancerGenomic instability disordersMitochondrial dysfunction (potential)
05

Safety considerations

Targeting EXD2 may risk impairing DNA repair, leading to genomic instability or sensitization to genotoxic stressPotential mitochondrial dysfunction if activity is inhibited

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