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. 2007 Aug 24;35(17):5789–5798. doi: 10.1093/nar/gkm503

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© 2007 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 6. — Models for the function of the archaeal homodimeric XPF (top) and human ERCC1/XPF heterodimer (bottom) constructed from the structure of the XPF homodimer bound to dsDNA (2bgw), the free structure of ERCC1/XPF C-terminal interacting domains (1z00) and the current structure of the ERCC1 central domain (2jpd). For the homodimer, one protomer is shown in a cartoon and the other in a surface representation. Accordingly, for the heterodimer ERCC1 is in a cartoon and XPF in a surface representation. The protein domains in both cases are colored as in Figure 1A.