Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
8401071 | Progress in Biophysics and Molecular Biology | 2015 | 6 Pages |
Abstract
BRCA1 BRCT domains function as phosphoprotein-binding modules for recognition of the phosphorylated protein-sequence motif pSXXF. While the motif interaction interface provides strong anchor points for binding, protein regions outside the motif have recently been found to be important for binding affinity. In this review, we compare the available structural data for BRCA1 BRCT domains in complex with phosphopeptides in order to gain a more complete understanding of the interaction between phosphopeptides and BRCA1-BRCT domains.
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Authors
Qian Wu, Harry Jubb, Tom L. Blundell,