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Article

Insights into the molecular basis of human hereditary breast cancer from studies of the BRCA1 BRCT domain.

Familial cancer - 1 Jan 2006

Glover J N Mark

Abstract excerpt

The C-terminal, BRCT repeats of BRCA1 are essential for the tumor suppressor function of this protein. Here we review structural and functional studies of this domain. Both repeats adopt similar folds and pack in an intimate, head-to-tail manner. The domain binds phosphorylated targets such as the DNA damage-associated kinase BACH1, with a specificity for pSer-X-X-Phe motifs. Structural studies reveal that the...

Read the complete abstract on PubMed

Topics

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Share to BRCA1 Protein
Share to DNA, Neoplasm
Share to DNA Repair

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Intracellular Signaling Peptides and Proteins

Share to Molecular Biology

Share to Mutation, Missense

Share to Neoplastic Syndromes, Hereditary

Share to Sensitivity and Specificity

Source

Identifiers

PMID: 16528612
DOI: 10.1007/s10689-005-2579-z

Genes

BRCA1
BACH1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

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Insights into the molecular basis of human hereditary breast cancer from studies of the BRCA1 BRCT domain.PMID 16528612Read ↗

Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer.Semantic proximity Read ↗

Crystal structure of the BRCT repeat region from the breast cancer-associated protein BRCA1.Semantic proximity Read ↗

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The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutationsSemantic proximity Read ↗

BRCA1 mutation spectrum, functions, and therapeutic strategies: The story so far.Semantic proximity Read ↗

Comprehensive analysis of missense variations in the BRCT domain of BRCA1 by structural and functional assays.Semantic proximity Read ↗

BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function.Semantic proximity Read ↗

New insights into the biological function of BRCA2 from its structural interactions.Semantic proximity Read ↗

Cancer predisposing mutations in BRCT domains.Semantic proximity Read ↗

Homologous repair of DNA damage and tumorigenesis: the BRCA connection.Semantic proximity Read ↗

Hereditary breast cancer and the BRCA1-associated FANCJ/BACH1/BRIP1.Semantic proximity Read ↗

Impact of RING and BRCT domain mutations on BRCA1 protein stability, localization and recruitment to DNA damage.Semantic proximity Read ↗

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