The BRCA1 C-terminal domain: structure and function

Mutat Res. 2000 Aug 30;460(3-4):319-32. doi: 10.1016/s0921-8777(00)00034-3.

Abstract

The BRCA1 C-terminal region contains a duplicated globular domain termed BRCT that is found within many DNA damage repair and cell cycle checkpoint proteins. The unique diversity of this domain superfamily allows BRCT modules to interact forming homo/hetero BRCT multimers, BRCT-non-BRCT interactions, and interactions with DNA strand breaks. The sequence and functional diversity of the BRCT superfamily suggests that BRCT domains are evolutionarily convenient interaction modules.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • BRCA1 Protein / chemistry*
  • BRCA1 Protein / physiology
  • Bacterial Proteins / chemistry
  • Biopolymers
  • Breast Neoplasms / genetics
  • Carrier Proteins / chemistry
  • Carrier Proteins / physiology
  • Cell Cycle Proteins / chemistry
  • DNA Damage
  • DNA Ligases / chemistry
  • DNA Nucleotidylexotransferase / chemistry
  • DNA Nucleotidylexotransferase / physiology
  • DNA Repair
  • DNA-Binding Proteins / chemistry
  • Evolution, Molecular
  • Female
  • Fungal Proteins / chemistry
  • Genes, BRCA1
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Mutation, Missense
  • Neoplastic Syndromes, Hereditary / genetics
  • Nuclear Proteins
  • Poly(ADP-ribose) Polymerases / chemistry
  • Protein Conformation
  • Protein Structure, Tertiary
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Structure-Activity Relationship
  • Tumor Suppressor Proteins*
  • Ubiquitin-Protein Ligases*
  • X-ray Repair Cross Complementing Protein 1

Substances

  • BRCA1 Protein
  • Bacterial Proteins
  • Biopolymers
  • Carrier Proteins
  • Cell Cycle Proteins
  • DNA-Binding Proteins
  • Fungal Proteins
  • Nuclear Proteins
  • TOPBP1 protein, human
  • Tumor Suppressor Proteins
  • X-ray Repair Cross Complementing Protein 1
  • XRCC4 protein, human
  • rad9 protein
  • BARD1 protein, human
  • Ubiquitin-Protein Ligases
  • Poly(ADP-ribose) Polymerases
  • DNA Nucleotidylexotransferase
  • DNA Ligases