ArticleMolecular cell2025
BRCA2 C-terminal clamp restructures RAD51 dimers to bind B-DNA for replication fork stability.
Article in Molecular cell, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- The BRCA1 coiled-coil domain is dispensable for suppression of tandem duplications and tolerance of FANCM loss.The EMBO journal · 2026Article
- Exploiting DNA damage tolerance for precision oncology.Trends in cancer · 2026Review
- R-loops and D-loops: a delicate balance in genomic stability and instability.Cell communication and signaling : CCS · 2026Review
- Structures and molecular mechanisms of RAD54B in modulating homologous recombination.bioRxiv : the preprint server for biology · 2026Article
- RF-SIRF reveals a replication stress-specific epigenetic code by spatio-temporal mapping of reversed forks.Nature communications · 2026Article
- Interplay Between Poly(ADP-ribosyl)ation and Specific Inner Cellular Events That Suggest Combination Strategies for Overcoming PARP Inhibitor Resistance.Pharmaceutics · 2026Review
- Cryo-electron microscopic visualization of RAD51 filament assembly and end-capping by XRCC3-RAD51C-RAD51D-XRCC2.Science (New York, N.Y.) · 2026Article
- EEPD1 evolved a unique DNA clamping dimer protecting reversed replication forks.Nucleic acids research · 2026Article
- The expanding roles of homologous recombination proteins in genome stability.The EMBO journal · 2026Review
- RAD51AP1 is a versatile RAD51 modulator.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
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18 authors.
Funding
Abstract
Tumor suppressor protein breast cancer susceptibility protein 2 (BRCA2) acts with RAD51 in replication fork protection (FP) and homology-directed DNA-break repair (HDR). Critical for cancer etiology and therapy resistance, the BRCA2 C terminus was thought to stabilize recombinogenic RAD51 after the assembly of ATP-extended RAD51 filaments on single-stranded DNA (ssDNA). Here, the detailed crystal structure of the human BRCA2 C-terminal interaction domain (TR2 interface [TR2i]) complexed with ATP-bound RAD51 prior to DNA binding instead reveals TR2i unexpectedly induces a unique ATP-RAD51 dimer conformation that accommodates nucleation onto double-stranded B-DNA unsuited for HDR initiation. Structural, biochemical, and molecular results with interface-guided mutations uncover TR2i's FP mechanism. Proline-driven secondary structure stabilizes residue triads and spans the RAD51 dimer, engaging pivotal interactions of RAD51 M210 and BRCA2 S3291/P3292, the cyclin-dependent kinase (CDK) phosphorylation site that toggles between FP during S phase and HDR in G2. TR2i evidently acts as an allosteric clamp, switching RAD51 from ssDNA to double-stranded and B-DNA binding, enforcing FP over HDR, challenging the current BRCA2-RAD51 dogma.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.