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

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-dimension...

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Detaylı Bibliyografya
Yayımlandı:	EMBO J
Asıl Yazarlar:	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.
Materyal Türü:	Artigo
Dil:	Inglês
Baskı/Yayın Bilgisi:	Nature Publishing Group 2003
Konular:	Articles
Online Erişim:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC202371/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/12941707/ https://ncbi.nlm.nih.govhttps://doi.org/10.1093/emboj/cdg429
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Full-length archaeal Rad51 structure and mutants: mechanisms for RAD51 assembly and control by BRCA2

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