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. 2005 Dec;13(12):1849-58.
doi: 10.1016/j.str.2005.08.014.

The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair

Konstantinos Tripsianes  1 , Gert Folkers, Eiso Ab, Devashish Das, Hanny Odijk, Nicolaas G J Jaspers, Jan H J Hoeijmakers, Robert Kaptein, Rolf Boelens
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Free article

The structure of the human ERCC1/XPF interaction domains reveals a complementary role for the two proteins in nucleotide excision repair

Konstantinos Tripsianes et al. Structure. 2005 Dec.
Free article

Abstract

The human ERCC1/XPF complex is a structure-specific endonuclease with defined polarity that participates in multiple DNA repair pathways. We report the heterodimeric structure of the C-terminal domains of both proteins responsible for ERCC1/XPF complex formation. Both domains exhibit the double helix-hairpin-helix motif (HhH)2, and they are related by a pseudo-2-fold symmetry axis. In the XPF domain, the hairpin of the second motif is replaced by a short turn. The ERCC1 domain folds properly only in the presence of the XPF domain, which implies a role for XPF as a scaffold for the folding of ERCC1. The intersubunit interactions are largely hydrophobic in nature. NMR titration data show that only the ERCC1 domain of the ERCC1/XPF complex is involved in DNA binding. On the basis of these findings, we propose a model for the targeting of XPF nuclease via ERCC1-mediated interactions in the context of nucleotide excision repair.

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  • Two blades of the [ex]scissor.
    Bunick CG, Chazin WJ. Bunick CG, et al. Structure. 2005 Dec;13(12):1740-1. doi: 10.1016/j.str.2005.11.003. Structure. 2005. PMID: 16338401 No abstract available.

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