title: BRCT domains: easy as one, two, three.
abstract: 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.
authors: Department of Biochemistry, University of Alberta, Edmonton, Alberta, Canada.
authors: Charles Chung Yun
authors: CC
authors: Leung
authors: J N Mark
authors: JN
authors: Glover
mesh_terms: D019313:BRCA1 Protein / Q000737:chemistry* / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000378:metabolism; D004260:DNA Repair; D010766:Phosphorylation; D011064:Poly Adenosine Diphosphate Ribose / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry / Q000378:metabolism
chemical_list: D019313:BRCA1 Protein; D016159:Tumor Suppressor Protein p53; D011064:Poly Adenosine Diphosphate Ribose; D004247:DNA