{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,2]],"date-time":"2026-10-02T22:22:56Z","timestamp":1790979776557,"version":"4.1.0"},"reference-count":83,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2007,10,2]],"date-time":"2007-10-02T00:00:00Z","timestamp":1191283200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[2008,3]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>The human XPF\u2010ERCC1 protein complex plays an essential role in nucleotide excision repair by catalysing positioned nicking of a DNA strand at the 5\u2032 side of the damage. We have recently solved the structure of the heterodimeric complex of the C\u2010terminal domains of XPF and ERCC1 (Tripsianes et al., Structure 2005;13:1849\u20131858). We found that this complex comprises a pseudo twofold symmetry axis and that the helix\u2013hairpin\u2013helix motif of ERCC1 is required for DNA binding, whereas the corresponding domain of XPF is functioning as a scaffold for complex formation with ERCC1. Despite the functional importance of heterodimerization, the C\u2010terminal domain of XPF can also form homodimers in vitro. We here compare the stabilities of homodimeric and heterodimeric complexes of the C\u2010terminal domains of XPF and ERCC1. The higher stability of the XPF HhH complexes under various experimental conditions, determined using CD and NMR spectroscopy and mass spectrometry, is well explained by the structural differences that exist between the HhH domains of the two complexes. The XPF HhH homodimer has a larger interaction interface, aromatic stacking interactions, and additional hydrogen bond contacts as compared to the XPF\/ERCC1 HhH complex, which accounts for its higher stability. Proteins 2008. \u00a9 2007 Wiley\u2010Liss, Inc.<\/jats:p>","DOI":"10.1002\/prot.21635","type":"journal-article","created":{"date-parts":[[2007,10,2]],"date-time":"2007-10-02T23:46:49Z","timestamp":1191368809000},"page":"1551-1563","source":"Crossref","is-referenced-by-count":20,"title":["The HhH domain of the human DNA repair protein XPF forms stable homodimers"],"prefix":"10.1002","volume":"70","author":[{"given":"Devashish","family":"Das","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Konstantinos","family":"Tripsianes","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Nicolaas G. 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