About half of all patients with hereditary breast or ovarian cancer have mutations in the BRCA1 gene. The huge, multifunctional 1,863 residue BRCA1 protein is suspected to play a role in DNA repair, control of cell division, and regulation of gene expression.

In the 26 September, 2001 issue of Nature Structural Biology, Professor Rachel Klevit and colleagues reported the NMR structure of the N-terminal RING domain of BRCA1 in complex with the RING domain of the protein BARD1. This is our first tantalizing glimpse of a key tumor suppressor protein.

For the complete story, see Brzovic, P. S., Rajagopal, P., Hoyt, D. W., King, M.-C. & Klevit, R. E. Structure of a BRCA1-BARD1 heterodimeric RING-RING complex. Nature Structural Biology, 8, 833-837, (2001).