BRCA1 C-terminal (BRCT) domains are integral signaling modules in the DNA damage response (DDR). Aside from their established roles as phospho-peptide binding modules, BRCT domains have been implicated in phosphorylation- independent protein interactions, DNA binding and poly(ADP-ribose) (PAR) binding. These numerous functions can be attributed to the diversity in BRCT domain structure and architecture, where domains can exist as isolated single domains or assemble into higher order homo- or hetero-domain complexes. In this review, we incorporate recent structural and biochemical studies to demonstrate how structural features allow single and tandem BRCT domains to attain a high degree of functional diversity. © 2011 Landes Bioscience.
CITATION STYLE
Leung, C. C. Y., & Glover, J. N. M. (2011). BRCT domains. Cell Cycle, 10(15), 2461–2470. https://doi.org/10.4161/cc.10.15.16312
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