title: The BRCA1 C-terminal domain: structure and function.
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.
authors.affiliation: Molecular Structure and Function, Imperial Cancer Research Fund, 44 Lincoln's Inn Fields, WC2A 3PX, London, UK.
authors.forename: T
authors.initials: T
authors.lastname: Huyton
authors.forename: P A
authors.initials: PA
authors.lastname: Bates
authors.forename: X
authors.initials: X
authors.lastname: Zhang
authors.forename: M J
authors.initials: MJ
authors.lastname: Sternberg
authors.forename: P S
authors.initials: PS
authors.lastname: Freemont
mesh_terms: D000595:Amino Acid Sequence; D019313:BRCA1 Protein / Q000737:chemistry* / Q000502:physiology; D001426:Bacterial Proteins / Q000737:chemistry; D001704:Biopolymers; D001943:Breast Neoplasms / Q000235:genetics; D002352:Carrier Proteins / Q000737:chemistry / Q000502:physiology; D018797:Cell Cycle Proteins / Q000737:chemistry; D004249:DNA Damage; D011088:DNA Ligases / Q000737:chemistry; D004253:DNA Nucleotidylexotransferase / Q000737:chemistry / Q000502:physiology; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000737:chemistry; D019143:Evolution, Molecular; D005260:Female; D005656:Fungal Proteins / Q000737:chemistry; D019398:Genes, BRCA1; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D020125:Mutation, Missense; D009386:Neoplastic Syndromes, Hereditary / Q000235:genetics; D009687:Nuclear Proteins; D011065:Poly(ADP-ribose) Polymerases / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship; D025521:Tumor Suppressor Proteins; D044767:Ubiquitin-Protein Ligases; D000076105:X-ray Repair Cross Complementing Protein 1
chemical_list: D019313:BRCA1 Protein; D001426:Bacterial Proteins; D001704:Biopolymers; D002352:Carrier Proteins; D018797:Cell Cycle Proteins; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D009687:Nuclear Proteins; C110513:TOPBP1 protein, human; D025521:Tumor Suppressor Proteins; D000076105:X-ray Repair Cross Complementing Protein 1; C101467:XRCC4 protein, human; C069930:rad9 protein; C102449:BARD1 protein, human; D044767:Ubiquitin-Protein Ligases; D011065:Poly(ADP-ribose) Polymerases; D004253:DNA Nucleotidylexotransferase; D011088:DNA Ligases