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Article

The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition.

Structure (London, England : 1993) - 4 Apr 2012

Das Devashish, Folkers Gert E, van Dijk Marc, Jaspers Nicolaas G J, Hoeijmakers Jan H J, Kaptein Robert, Boelens Rolf

Abstract excerpt

Human XPF/ERCC1 is a structure-specific DNA endonuclease that nicks the damaged DNA strand at the 5' end during nucleotide excision repair. We determined the structure of the complex of the C-terminal domain of XPF with 10 nt ssDNA. A positively charged region within the second helix of the first HhH motif contacts the ssDNA phosphate backbone. One guanine base is flipped out of register and positioned in a...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22483113
DOI: 10.1016/j.str.2012.02.009

Genes

ERCC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition.PMID 22483113Read ↗

Function and Interactions of ERCC1-XPF in DNA Damage ResponseSemantic proximity Read ↗

The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision RepairSemantic proximity Read ↗

Multiple DNA binding domains mediate the function of the ERCC1-XPF protein in nucleotide excision repair.Semantic proximity Read ↗

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

Cryo-EM Structures of the XPF-ERCC1 Endonuclease Reveal an Auto-Inhibited Conformation and the Basis for ActivationSemantic proximity Read ↗

The interaction of XPG with TFIIH through p62 and XPD is required for the completion of nucleotide excision repair.Semantic proximity Read ↗

Structural basis for the recruitment of ERCC1-XPF to nucleotide excision repair complexes by XPA.Semantic proximity Read ↗

Physical and Functional Interaction between the XPF/ERCC1 Endonuclease and hRad52Semantic proximity Read ↗

Mapping of interaction domains between human repair proteins ERCC1 and XPFSemantic proximity Read ↗

Structural and functional analyses of an archaeal XPF/Rad1/Mus81 nuclease: asymmetric DNA binding and cleavage mechanisms.Semantic proximity Read ↗

Processing of branched DNA intermediates by a complex of human FEN-1 and PCNASemantic proximity Read ↗

The TFIIH subunits p44/p62 act as a damage sensor during nucleotide excision repairSemantic proximity Read ↗

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