These tools will no longer be maintained as of December 31, 2024. Archived website can be found here. PubMed4Hh GitHub repository can be found here. Contact NLM Customer Service if you have questions.


PUBMED FOR HANDHELDS

Search MEDLINE/PubMed


  • Title: Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif.
    Author: Wu Q, Jubb H, Blundell TL.
    Journal: Prog Biophys Mol Biol; 2015 Mar; 117(2-3):143-148. PubMed ID: 25701377.
    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.
    [Abstract] [Full Text] [Related] [New Search]