Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains.

  title={Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains.},
  author={Maria Victoria E Botuyan and Yves Nomin{\'e} and Xiaochun Yu and Nenad O. Juranic and Slobodan Macura and Junjie Chen and Georges Mer},
  volume={12 7},
BRCT tandem domains, found in many proteins involved in DNA damage checkpoint and DNA repair pathways, were recently shown to be phosphopeptide binding motifs. Using solution nuclear magnetic resonance (NMR) spectroscopy and mutational analysis, we have characterized the interaction of BRCA1-BRCT domains with a phosphoserine-containing peptide derived from the DNA repair helicase BACH1. We show that a phenylalanine in the +3 position from the phosphoserine of BACH1 is bound to a conserved… CONTINUE READING


Publications citing this paper.
Showing 1-10 of 30 extracted citations

Structural characterization of BRCT-tetrapeptide binding interactions.

Biochemical and biophysical research communications • 2010
View 8 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…