The BRCT Domain Is a Phospho-Protein Binding Domain

@article{Yu2003TheBD,
  title={The BRCT Domain Is a Phospho-Protein Binding Domain},
  author={Xiaochun Yu and Claudia Christiano Silva Chini and Miao He and Georges Mer and Junjie Chen},
  journal={Science},
  year={2003},
  volume={302},
  pages={639 - 642}
}
The carboxyl-terminal domain (BRCT) of the Breast Cancer Gene 1 (BRCA1) protein is an evolutionarily conserved module that exists in a large number of proteins from prokaryotes to eukaryotes. Although most BRCT domain–containing proteins participate in DNA-damage checkpoint or DNA-repair pathways, or both, the function of the BRCT domain is not fully understood. We show that the BRCA1 BRCT domain directly interacts with phosphorylated BRCA1-Associated Carboxyl-terminal Helicase (BACH1). This… 

A Proteomic Approach to Identify Phosphorylation-Dependent Targets of BRCT Domains

The results suggest that the BRCT domain acts as a sensor to protein phosphorylation in response to DNA damage, recruits phosphorylated cellular targets, and mediates signaling complex formation, suggesting a more global role of BRCT domains in genome stability surveillance.

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

Structural basis for phosphorylation-dependent signaling in the DNA-damage response.

The studies have revealed a flexible mode of recognition that allows PNK to interact with numerous negatively charged substrates, and a secondary binding pocket at the interface between tandem repeats, which recognizes the amino-acid 3 residues C-terminal to the phosphoserine.

SYNTHÈSE Structural basis for phosphorylation-dependent signaling in the DNA-damage response 1

The studies have revealed a flexible mode of recognition that allows PNK to interact with numerous negatively charged substrates, and a secondary binding pocket at the interface between tandem repeats, which recognizes the amino-acid 3 residues C-terminal to the phosphoserine.

BRCT domains: phosphopeptide binding and signaling modules.

This review seeks to discuss the recent biochemical and structural data that have helped elucidate the molecular basis of BRCT domain function and BRCT-mediated interactions, with special emphasis on the role of phospho-specific interactions in key networks that regulate DNA repair.

Characterization of the DNA Binding and Structural Properties of the BRCT region of the p140 subunit of human Replication Factor C

  • Biology
  • 2006
It is demonstrated that a region of p140 that encompasses the BRCT domain contains two distinct DNA binding activities, and a larger polypeptide incorporating these sequences (375-545) is well ordered even in the absence of the DNA ligand.

Tandem BRCT Domains: DNA's Praetorian Guard.

Emerging views of the origin and evolving roles of tandem BRCT domain repeats in the DNA damage response are discussed.
...

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