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Article

Structural mechanism of the phosphorylation-dependent dimerization of the MDC1 forkhead-associated domain.

Nucleic acids research - 1 May 2012

Liu Jinping, Luo Shukun, Zhao Hongchang, Liao Ji, Li Jing, Yang Chunying, Xu Bo, Stern David F, Xu Xingzhi, Ye Keqiong

Abstract excerpt

MDC1 is a key mediator of the DNA-damage response in mammals with several phosphorylation-dependent protein interaction domains. The function of its N-terminal forkhead-associated (FHA) domain remains elusive. Here, we show with structural, biochemical and cellular data that the FHA domain mediates phosphorylation-dependent dimerization of MDC1 in response to DNA damage. Crystal structures of the FHA domain...

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Source

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Identifiers

PMID: 22234877
DOI: 10.1093/nar/gkr1296
PMCID: PMC3351156

Genes

MDC1
ATM

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.

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