Decoding the Structural Basis of DNA Polymerase θ Function to Unlock Novel Cancer Therapeutics
- Unveiling the cryo-EM structures of Polθ helicase bound to DNA and how structural rearrangements facilitate error-prone double-strand break repair
- Positioning 3′ single-stranded DNA ends to align complementary bases
- Highlighting structural determinants and potential allosteric sites for therapeutic intervention
- How structure-guided drug discovery is advancing first-in-class Polθ inhibitors to address DNA repair vulnerabilities in cancer