Close-up on breast cancer protein

High-resolution structures of the N- and C-terminal regions of BRCA1 show cancer-predisposing mutations may affect the domain.

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Mutations in the tumor suppressor BRCA1 gene that affects the N- and C-terminal regions of the protein are implicated with a high risk of developing breast cancer. Two papers in October Nature Structural Biology describe the high-resolution structures of the N- and C-terminal regions of BRCA1 protein and show how the cancer-predisposing mutations may affect the architecture of these domains.

In the first paper, Rachel Klevit and colleagues from the University of Washington at Seattle, USA, report the three-dimensional structure of the N-terminal region of BRCA1 (called the RING domain) in complex with the RING domain of a BARD1 protein. This illustrates how the BRCA1 can associate with multiple protein partners and reveals the effects of cancer mutations at a molecular level (Nature Struct Biol 2001, 8:833-837).

In the second paper, Scott Williams and colleagues from University of Alberta at Edmonton, Canada, report the crystal structure of the C-terminal region ...

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