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Article

Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2.

The EMBO journal - 1 Sept 2003

Shin David S, Pellegrini Luca, Daniels Douglas S, Yelent Biana, Craig Lisa, Bates Debbie, Yu David S, Shivji Mahmud K, Hitomi Chiharu, Arvai Andrew S, Volkmann Niels, Tsuruta Hiro, Blundell Tom L, Venkitaraman Ashok R, Tainer John A

Abstract excerpt

To clarify RAD51 interactions controlling homologous recombination, we report here the crystal structure of the full-length RAD51 homolog from Pyrococcus furiosus. The structure reveals how RAD51 proteins assemble into inactive heptameric rings and active DNA-bound filaments matching three-dimensional electron microscopy reconstructions. A polymerization motif (RAD51-PM) tethers individual subunits together to...

Read the complete abstract on PubMed

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Crystallography, X-Ray

Share to Microscopy, Electron

Share to Protein Structure, Quaternary

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Source

Open in PubMed Open full text

Identifiers

PMID: 12941707
DOI: 10.1093/emboj/cdg429
PMCID: PMC202371

Genes

RAD51
BRCA2
RAD52

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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