A university of Alberta biochemist has recreated the three-dimensional structure of a critical portion of the BRCA1 protein, which if mutated, causes, hereditary breast cancer.Using ultra-sensitive x-ray crystallography, biochemistry assistant professor Mark Glover has uncovered the three dimensional structure of an important part of the breast cancer-associated protein, BRCA1.
Mutations in BRCA1 cause about half of all hereditary breat cancers. The structure may give clinicians the ability to formulate genetic screening programs to identifyt women at risk for the deadly disease.
The finely detailed images, will give researchers new clues on how the crucial protein effectively prevents cells from becoming cancerous.
The protein is enormous in size and scope, with a chain of some 1,863 amino acids that comprises a complex, three-dimensional structure.Scientists have been focusing their investigations on the two ends of the protein, the C terminus and the N terminus.The focus of Glover's work has been the C-terminus, which consits of a pair of related structures, called BRCT repeats.
BRCT repeats not only occur in BRCA1, but are a hallmark of a large family of proteins which play a role in the repair of DNA damage.Researchers know that the ends of the complex protein are particularly susceptible to mutations implicated in breast and ovarian cancer.A team of researchers led by University of Washington professor Rachel Klevit, using nuclear magnetic resonance imaging techniques, has been focusing its investigations on the N terminus.