ArticleNucleic acids research2013
Contributions of the RAD51 N-terminal domain to BRCA2-RAD51 interaction.
Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 44 citations in OpenAlex.
- Structural insight into how RAD51 paralog exchange regulates RAD51 filament formation.Nature structural & molecular biology · 2026Article
- Dissecting the RAD51-BRC4 Interaction Landscape through Integrative Molecular Simulations and Experimental Biophysics.Journal of chemical information and modeling · 2025Article
- BRCA2 C-terminal clamp restructures RAD51 dimers to bind B-DNA for replication fork stability.Molecular cell · 2025Article
- Article
- The human Shu complex promotes RAD51 activity by modulating RPA dynamics on ssDNA.Nature communications · 2024Article
- Natural variation of codon repeats inScience advances · 2023Article
- Improved RAD51 binders through motif shuffling based on the modularity of BRC repeats.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Identification and analysis of genes associated with epithelial ovarian cancer by integrated bioinformatics methods.PloS one · 2021Article
- RADX condenses single-stranded DNA to antagonize RAD51 loading.Nucleic acids research · 2020Article
- Structural basis of homologous recombination.Cellular and molecular life sciences : CMLS · 2020Review
- A novel UCHLCell death & disease · 2019Article
- Determinants of human glucokinase activation and implications for small molecule allosteric control.Biochimica et biophysica acta. General subjects · 2018Article
- Integrating Experimental and In Silico HTS in the Discovery of Inhibitors of Protein-Nucleic Acid Interactions.Methods in enzymology · 2018Article
- Observation and Analysis of RAD51 Nucleation Dynamics at Single-Monomer Resolution.Methods in enzymology · 2018Article
- Expression, Purification, and Biochemical Evaluation of Human RAD51 Protein.Methods in enzymology · 2018Article
- Variation in RAD51 details a hub of functions: opportunities to advance cancer diagnosis and therapy.F1000Research · 2018Review
- Small-Molecule Inhibitors Targeting DNA Repair and DNA Repair Deficiency in Research and Cancer Therapy.Cell chemical biology · 2017Review
- A phosphorylation-deubiquitination cascade regulates the BRCA2-RAD51 axis in homologous recombination.Genes & development · 2016Article
- Engineering Archeal Surrogate Systems for the Development of Protein-Protein Interaction Inhibitors against Human RAD51.Journal of molecular biology · 2016Article
- High-resolution structure of the presynaptic RAD51 filament on single-stranded DNA by electron cryo-microscopy.Nucleic acids research · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
RAD51 DNA strand exchange protein catalyzes the central step in homologous recombination, a cellular process fundamentally important for accurate repair of damaged chromosomes, preservation of the genetic integrity, restart of collapsed replication forks and telomere maintenance. BRCA2 protein, a product of the breast cancer susceptibility gene, is a key recombination mediator that interacts with RAD51 and facilitates RAD51 nucleoprotein filament formation on single-stranded DNA generated at the sites of DNA damage. An accurate atomistic level description of this interaction, however, is limited to a partial crystal structure of the RAD51 core fused to BRC4 peptide. Here, by integrating homology modeling and molecular dynamics, we generated a structure of the full-length RAD51 in complex with BRC4 peptide. Our model predicted previously unknown hydrogen bonding patterns involving the N-terminal domain (NTD) of RAD51. These interactions guide positioning of the BRC4 peptide within a cavity between the core and the NTDs; the peptide binding separates the two domains and restricts internal dynamics of RAD51 protomers. The model's depiction of the RAD51-BRC4 complex was validated by free energy calculations and in vitro functional analysis of rationally designed mutants. All generated mutants, RAD51(E42A), RAD51(E59A), RAD51(E237A), RAD51(E59A/E237A) and RAD51(E42A/E59A/E237A) maintained basic biochemical activities of the wild-type RAD51, but displayed reduced affinities for the BRC4 peptide. Strong correlation between the calculated and experimental binding energies confirmed the predicted structure of the RAD51-BRC4 complex and highlighted the importance of RAD51 NTD in RAD51-BRCA2 interaction.
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Registered trials
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