The BRCA1 C-terminal domain: structure and function

• Published in: Mutation research Vol. 460; no. 3-4; pp. 319 - 332
• Main Authors: Huyton, Trevor, Bates, Paul A, Zhang, Xiaodong, Sternberg, Michael J.E, Freemont, Paul S
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 30.08.2000
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Biopolymers; BRCA1; BRCA1 protein; BRCA1 Protein - chemistry; BRCA1 Protein - physiology; BRCT; Breast Neoplasms - genetics; Carrier Proteins - chemistry; Carrier Proteins - physiology; Cell Cycle Proteins - chemistry; DNA Damage; DNA damage repair; 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 interaction module; 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; XRCC1; DNA damage repair; XRCC1; BRCA1; Protein interaction module; BRCT
• ISSN: 0921-8777; 0027-5107; 1386-1476
• DOI: 10.1016/S0921-8777(00)00034-3

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.