期刊
CELL CYCLE
卷 10, 期 15, 页码 2461-2470出版社
LANDES BIOSCIENCE
DOI: 10.4161/cc.10.15.16312
关键词
BRCT domain; DNA repair; phosphorylation; phospho-peptide interaction; protein interaction; DNA binding; DNA damage response
类别
资金
- Canadian Cancer Society
- National Institutes of Health
- Howard Hughes Medical Institute
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.
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