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. 2017 Aug 25;45(18):10872–10883. doi: 10.1093/nar/gkx743

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© The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 5. — Cartoon representation depicting the summary of our observations with the same coloring scheme as used in Figure 1 showing core-TFIIH with XPD. Left panel: wild-type active TFIIH. Middle panel: TFIIH mutated within the minimal p34/p44 interface (structurally characterized in this study) maintaining the active complex. Right panel: TFIIH with the C4 domain of p34 missing. This p34 variant still interacts with p44 but other vital interactions are missing leading to an inactive TFIIH.