{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,3]],"date-time":"2026-10-03T21:15:57Z","timestamp":1791062157468,"version":"4.1.0"},"reference-count":41,"publisher":"National Academy of Sciences","issue":"32","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2005,8,9]]},"abstract":"<jats:p>\n                    Human XPF\u2013ERCC1 is a DNA endonuclease that incises a damaged DNA strand on the 5\u2032 side of a lesion during nucleotide excision repair and has additional role(s) in homologous recombination and DNA interstrand crosslink repair. We show that a truncated form of XPF lacking the N-terminal helicase-like domain in complex with ERCC1 exhibits a structure-specific endonuclease activity with similar specificity to that of full-length XPF\u2013ERCC1. Two domains of ERCC1, a central domain and a C-terminal tandem helix\u2013hairpin\u2013helix (HhH\n                    <jats:sub>2<\/jats:sub>\n                    ) dimerization domain, bind to ssDNA. The central domain of ERCC1 binds ssDNA\/dsDNA junctions with a defined polarity, preferring a 5\u2032 single-stranded overhang. The XPF\u2013ERCC1 HhH\n                    <jats:sub>2<\/jats:sub>\n                    domain heterodimer contains two independent ssDNA-binding surfaces, which are revealed by a crystal structure of the protein complex. A crystal structure of the central domain of ERCC1 shows its fold is strikingly similar to that of the nuclease domains of the archaeal Mus81\/XPF homologs, despite very low sequence homology. A groove lined with basic and aromatic residues on the surface of ERCC1 has apparently been adapted to interact with ssDNA. On the basis of these crystallographic and biochemical studies, we propose a model in which XPF\u2013ERCC1 recognizes a branched DNA substrate by binding the two ssDNA arms with the two HhH\n                    <jats:sub>2<\/jats:sub>\n                    domains of XPF and ERCC1 and by binding the 5\u2032-ssDNA arm with the central domain of ERCC1.\n                  <\/jats:p>","DOI":"10.1073\/pnas.0504341102","type":"journal-article","created":{"date-parts":[[2005,8,2]],"date-time":"2005-08-02T22:54:01Z","timestamp":1123023241000},"page":"11236-11241","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":146,"title":["Crystal structure and DNA binding functions of ERCC1, a subunit of the DNA structure-specific endonuclease XPF\u2013ERCC1"],"prefix":"10.1073","volume":"102","author":[{"given":"Oleg V.","family":"Tsodikov","sequence":"first","affiliation":[{"name":"Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115; and Institute of Molecular Cancer Research, University of Z\u00fcrich, Winterthurerstrasse 190, 8057 Z\u00fcrich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacquelin H.","family":"Enzlin","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115; and Institute of Molecular Cancer Research, University of Z\u00fcrich, Winterthurerstrasse 190, 8057 Z\u00fcrich, Switzerland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Orlando D.","family":"Sch\u00e4rer","sequence":"additional","affiliation":[{"name":"Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 240 Longwood Avenue, Boston, MA 02115; and Institute of Molecular Cancer Research, University of Z\u00fcrich, Winterthurerstrasse 190, 8057 Z\u00fcrich, 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