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. 2017 Nov 27;7:16428. doi: 10.1038/s41598-017-16681-y

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© The Author(s) 2017

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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Structural basis of the DNA recognition by 71F12. (A–C) Structure of the 71F12 Fab-DNA complex determined by crystallography. The DNA-binding sites (sites 1–3, B). Thymine bases (T₀, T₋₁, and T₋₂, C). Hydrogen bonds are denoted by dashed magenta lines. (D and E) Replacement of F33 (D: magenta) with Y33 (E: cyan) would cause steric hindrance (dashed line). (F and G) Sequences of the 71F12 heavy chain (F) and light chain (G). The contacting residues are boxed. For the heavy chain, the conservation of each position from the HTS is shown below as gray bars, except for the three conserved mutations colored in red. (H and I) The 71F12 IgH-GL antibodies with indicated mutations were tested in SPR for the interaction with 5′-TTTTT-3′ (H), or 9-mer DNAs with the indicated sequences (I). The mean values of K_D ± s.e.m. from three experiments are shown.