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Article

Crystal structure of human XLF: a twist in nonhomologous DNA end-joining.

Molecular cell - 28 Dec 2007

Andres Sara N, Modesti Mauro, Tsai Chun J, Chu Gilbert, Junop Murray S

Abstract excerpt

DNA double-strand breaks represent one of the most severe forms of DNA damage in mammalian cells. One pathway for repairing these breaks occurs via nonhomologous end-joining (NHEJ) and depends on XRCC4, LigaseIV, and Cernunnos, also called XLF. Although XLF stimulates XRCC4/LigaseIV to ligate mismatched and noncohesive DNA ends, the mechanistic basis for this function remains unclear. Here we report the structure...

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

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Source

Identifiers

PMID: 18158905
DOI: 10.1016/j.molcel.2007.10.024

Genes

XRCC4

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

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Crystal structure of human XLF: a twist in nonhomologous DNA end-joining.PMID 18158905Read ↗

Structural characterization of filaments formed by human Xrcc4-Cernunnos/XLF complex involved in nonhomologous DNA end-joining.Semantic proximity Read ↗

XLF interacts with the XRCC4-DNA ligase IV complex to promote DNA nonhomologous end-joining.Semantic proximity Read ↗

Length-dependent binding of human XLF to DNA and stimulation of XRCC4.DNA ligase IV activity.Semantic proximity Read ↗

Evolutionary and functional conservation of the DNA non-homologous end-joining protein, XLF/Cernunnos.Semantic proximity Read ↗

The spatial organization of non-homologous end joining: From bridging to end joiningSemantic proximity Read ↗

PAXX binding to the NHEJ machinery explains functional redundancy with XLFSemantic proximity Read ↗

XRCC4's interaction with XLF is required for coding (but not signal) end joining.Semantic proximity Read ↗

Functional significance of the interaction with Ku in DNA double-strand break recognition of XLF.Semantic proximity Read ↗

Structural and Functional Interaction between the Human DNA Repair Proteins DNA Ligase IV and XRCC4Semantic proximity Read ↗

Cooperative assembly of a protein-DNA filament for nonhomologous end joining.Semantic proximity Read ↗

PAXX, a paralog of XRCC4 and XLF, interacts with Ku to promote DNA double-strand break repairSemantic proximity Read ↗

Interplay between Cernunnos-XLF and Nonhomologous End-joining Proteins at DNA Ends in the CellSemantic proximity Read ↗

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