Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif

Prog Biophys Mol Biol. 2015 Mar;117(2-3):143-148. doi: 10.1016/j.pbiomolbio.2015.02.003. Epub 2015 Feb 17.

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.

Keywords: BRCA1; BRCT; DNA damage response; Phosphopeptide; Tandem BRCT domains; pSXXF motif.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • BRCA1 Protein / chemistry*
  • BRCA1 Protein / metabolism
  • BRCA1 Protein / ultrastructure*
  • Binding Sites
  • Computer Simulation
  • DNA Damage / physiology*
  • DNA Repair / physiology
  • Models, Chemical*
  • Models, Molecular*
  • Molecular Sequence Data
  • Phosphopeptides / chemistry*
  • Phosphopeptides / metabolism
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Tertiary

Substances

  • BRCA1 Protein
  • Phosphopeptides