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. 2018 Jul 6;9:2642. doi: 10.1038/s41467-018-05024-8

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 8 — Structural insights into LIG4 syndrome mutations and polymorphisms. a Known LIG4 syndrome mutations (residues in space-filling representation, hot pink) mapped onto the LigIV closed DNA–adenylate structure (protein in purple, DNA in green). b Relative positions of mutations near the AMP (cyan) binding site of human LigIV that have been associated with LigIV deficiency. c Conformation of the LigIV N-terminus (orange), and its putative role in protein folding and stability. Thr9 makes a putative hydrogen bond with Gln146, which could be disrupted when mutated to isoleucine. d Disposition of residues in Motif Va (magenta, with Gly469 in red), in relation to the bound DNA substrate (green)