title: Phosphopeptide interactions with BRCA1 BRCT domains: More than just a motif.
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.
authors.affiliation: Department of Biochemistry, 80 Tennis Court Road, University of Cambridge, CB2 1GA, Cambridge, United Kingdom. Electronic address: qw222@cam.ac.uk.
authors.forename: Qian
authors.initials: Q
authors.lastname: Wu
authors.affiliation: Department of Biochemistry, 80 Tennis Court Road, University of Cambridge, CB2 1GA, Cambridge, United Kingdom.
authors.forename: Harry
authors.initials: H
authors.lastname: Jubb
authors.affiliation: Department of Biochemistry, 80 Tennis Court Road, University of Cambridge, CB2 1GA, Cambridge, United Kingdom.
authors.forename: Tom L
authors.initials: TL
authors.lastname: Blundell
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D019313:BRCA1 Protein / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure*; D001665:Binding Sites; D003198:Computer Simulation; D004249:DNA Damage / Q000502:physiology*; D004260:DNA Repair / Q000502:physiology; D008956:Models, Chemical; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010748:Phosphopeptides / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary
chemical_list: D019313:BRCA1 Protein; D010748:Phosphopeptides
keywords: BRCA1; BRCT; DNA damage response; Phosphopeptide; Tandem BRCT domains; pSXXF motif