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 and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2.

Molecular cell - 1 May 2002

Li Jiejin, Williams Brandi L, Haire Lesley F, Goldberg Michal, Wilker Erik, Durocher Daniel, Yaffe Michael B, Jackson Stephen P, Smerdon Stephen J

Abstract excerpt

The Chk2 Ser/Thr kinase plays crucial, evolutionarily conserved roles in cellular responses to DNA damage. Identification of two pro-oncogenic mutations within the Chk2 FHA domain has highlighted its importance for Chk2 function in checkpoint activation. The X-ray structure of the Chk2 FHA domain in complex with an in vitro selected phosphopeptide motif reveals the determinants of binding specificity and shows...

Read the complete abstract on PubMed

Topics

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

Share to BRCA1 Protein
Share to Checkpoint Kinase 2

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Forkhead Transcription Factors

Share to Peptide Library

Share to Peptide Mapping

Share to Protein Kinases

Share to Smad Proteins

Source

Identifiers

PMID: 12049740
DOI: 10.1016/s1097-2765(02)00527-0

Genes

ATM
BRCA1

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional versatility of the FHA domain in DNA-damage signaling by the tumor suppressor kinase Chk2.PMID 12049740Read ↗

Structure and activation mechanism of the CHK2 DNA damage checkpoint kinase.Semantic proximity Read ↗

Phosphorylation of threonine 68 promotes oligomerization and autophosphorylation of the Chk2 protein kinase via the forkhead-associated domain.Semantic proximity Read ↗

The molecular basis of ATM-dependent dimerization of the Mdc1 DNA damage checkpoint mediatorSemantic proximity Read ↗

The hCds1 (Chk2)-FHA domain is essential for a chain of phosphorylation events on hCds1 that is induced by ionizing radiation.Semantic proximity Read ↗

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

The Chk2 protein kinase.Semantic proximity Read ↗

MDC1 is coupled to activated CHK2 in mammalian DNA damage response pathways.Semantic proximity Read ↗

Chk2 activation and phosphorylation-dependent oligomerization.Semantic proximity Read ↗

FHA Domains as Phospho‐Threonine Binding Modules in Cell SignalingSemantic proximity Read ↗

Characterization of tumor-associated Chk2 mutations.Semantic proximity Read ↗

CHK2 kinase--a busy messenger.Semantic proximity Read ↗

DNA damage regulates Chk2 association with chromatin.Semantic proximity Read ↗

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