Abstract
The BRCA1 C-terminus (BRCT) domains are essential for the tumor suppressor function of BRCA1, and have been found in a variety of proteins from bacteria to men. Recent studies demonstrate that the BRCT domain constitutes a novel phosphopeptide binding region. In this review we seek to discuss the recent biochemical and structural data that have helped elucidate the molecular basis of BRCT domain function and BRCT-mediated interactions, with special emphasis on the role of phosphospecific interactions in key networks that regulate DNA repair. Finally we offer predictions on additional phosphointeracting BRCT domains and potential in vivo binding sites for several BRCT domains.
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Rodriguez, M. C., & Zhou, S. (2008, May 1). BRCT domains: Phosphopeptide binding and signaling modules. Frontiers in Bioscience. Bioscience Research Institute. https://doi.org/10.2741/3125
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