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Breast cancer is one of the most common and deadly forms of cancer in women. In the U.S. alone, ~18,000 women are diagnosed annually. One of the risk factors for this disease is mutation in the tumor suppressor protein BRCA1. Mutations in BRCA1 are linked to the familial and early onset forms of breast cancer and affect ~5% of the patients suffering from this disease. These mutations often occur in the N- and C-terminal regions of BRCA1, which are essential for its function.
BRCA1 is involved in a variety of cellular processes, such as DNA repair, and appears to be important in maintaining genome integrity. While scientists are beginning to understand the cellular functions of BRCA1, the molecular basis for the mutations that predispose women for breast cancer is not clear. To address this deficiency, two groups of researchers report in this issue of Nature Structural Biology (Vol. 8, No. 10, 01 Oct 2001) the high-resolution structures of the N- and C-terminal regions of BRCA1. In one paper (pp. 833-837), Rachel Klevit and coworkers at the University of Washington at Seatle, USA, describe the solution structure of the N-terminal region of BRCA1, called the RING domain, in complex with the RING domain from a BRCA1-associated protein called BARD1. In the second paper (pp. 838-842), Mark Glover and colleagues of the University of Alberta at Edmonton, Canada, report the crystal structure of the C-terminal region of BRCA1 called the BRCT repeat. The locations of the cancer-predisposing mutations within these structures suggest that the mutations may affect the architecture of the domains and thus compromise the tumor-suppressing activities of BRCA1. Richard Baer of the Columbia University discusses these findings in an associated News and Views (pp. 822-824). Contact information:
Dr. Rachel E. Klevit
University of Washington
Department of Biochemistry
Biomolecular Structure Center
Box 357742
Seattle, Washington 98195-7742
USA
Tel: 206 543 5891
Fax: 206 543 8394
Email: klevit@u.washington.edu Dr. J. N. Mark Glover
University of Alberta
Department of Biochemistry
474 Medical Sciences Building
Edmonton, T6G 2H7
Canada
Tel: 780 492 2136
Fax: 780 492 0886
Email: mark.glover@ualberta.ca Dr. Richard Baer
Columbia University
Department of Pathology
New York, New York 10032
USA
Tel: 212 304 7382
Fax: 212 304 7336
Email: rb670@columbia.edu (C) Nature Structural Biology press release.
Message posted by: Trevor M. D'Souza
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