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...

Full description

Bibliographic Details

Published in:	EMBO J
Main Authors:	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.
Format:	Artigo
Language:	Inglês
Published:	Nature Publishing Group 2003
Subjects:	Articles
Online Access:	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
Tags:	Add Tag No Tags, Be the first to tag this record!