Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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

Structure (London, England : 1993) - 1 Jul 2004

Botuyan Maria Victoria E, Nominé Yves, Yu Xiaochun, Juranic Nenad, Macura Slobodan, Chen Junjie, Mer Georges

Abstract excerpt

BRCT tandem domains, found in many proteins involved in DNA damage checkpoint and DNA repair pathways, were recently shown to be phosphopeptide binding motifs. Using solution nuclear magnetic resonance (NMR) spectroscopy and mutational analysis, we have characterized the interaction of BRCA1-BRCT domains with a phosphoserine-containing peptide derived from the DNA repair helicase BACH1. We show that a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Basic-Leucine Zipper Transcription Factors
Share to BRCA1 Protein

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

Share to Carrier Proteins

Share to Culture Media

Share to Fanconi Anemia Complementation Group Proteins

Share to Magnetic Resonance Spectroscopy

Share to Protein Structure, Tertiary

Share to Tumor Cells, Cultured

Source

Open in PubMed Open full text

Identifiers

PMID: 15242590
DOI: 10.1016/j.str.2004.06.002
PMCID: PMC3652423

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains.PMID 15242590Read ↗

BRCT domains: phosphopeptide binding and signaling modules.Semantic proximity Read ↗

Structural basis of phosphopeptide recognition by the BRCT domain of BRCA1.Semantic proximity Read ↗

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

The BRCT domain is a phospho-protein binding domain.Semantic proximity Read ↗

Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains.Semantic proximity Read ↗

The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms.Semantic proximity Read ↗

Cancer-related mutations in BRCA1-BRCT cause long-range structural changes in protein-protein binding sites: a molecular dynamics study.Semantic proximity Read ↗

Comparison of the structures and peptide binding specificities of the BRCT domains of MDC1 and BRCA1.Semantic proximity Read ↗

Distinct Mechanisms of Recognition of Phosphorylated RNAPII C-Terminal Domain by BRCT Repeats of the BRCA1–BARD1 Complex: Insights from Structural and Functional AnalysesSemantic proximity Read ↗

BRCT domains of the DNA damage checkpoint proteins TOPBP1/Rad4 display distinct specificities for phosphopeptide ligandsSemantic proximity Read ↗

A supramodular FHA/BRCT-repeat architecture mediates Nbs1 adaptor function in response to DNA damage.Semantic proximity Read ↗

Structural and functional analysis of the Crb2-BRCT2 domain reveals distinct roles in checkpoint signaling and DNA damage repair.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.