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Article

Cryo-EM structures of the XPF-ERCC1 endonuclease reveal how DNA-junction engagement disrupts an auto-inhibited conformation.

Nature communications - 28 Feb 2020

Jones Morgan, Beuron Fabienne, Borg Aaron, Nans Andrea, Earl Christopher P, Briggs David C, Snijders Ambrosius P, Bowles Maureen, Morris Edward P, Linch Mark, McDonald Neil Q

Abstract excerpt

The structure-specific endonuclease XPF-ERCC1 participates in multiple DNA damage repair pathways including nucleotide excision repair (NER) and inter-strand crosslink repair (ICLR). How XPF-ERCC1 is catalytically activated by DNA junction substrates is not currently understood. Here we report cryo-electron microscopy structures of both DNA-free and DNA-bound human XPF-ERCC1. DNA-free XPF-ERCC1 adopts an...

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Identifiers

PMID: 32111838
DOI: 10.1038/s41467-020-14856-2
PMCID: PMC7048804

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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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