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. 2020 Mar 4;10:4053. doi: 10.1038/s41598-020-61030-1

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© The Author(s) 2020

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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Interaction of MeCP2 Rett mutants. (a) Protein architecture of MeCP2 and positions of studied mutations. (b) Rett mutations highlighted on MeCP2 in complex with mC/mC containing DNA (PDB entry 3C2I⁴⁹. Prepared with UCSF ChimeraX⁵⁰. (c–f) Bar diagrams of the fraction of MBD-bound DNA duplex observed in EMSA for MBDs at 1,024 nM and nucleobase combinations as indicated in dark grey; data for wildtype hMeCP2[90–181] underlaid in light gray for comparison. Data are means ± SEM from three independent experiments (see SI for full data). (g) K_d log diagrams of wildtype and Rett mutants. (h) Table of K_d values obtained from measurements in (g). (i) Fold-loss in affinity (on basis of K_d) for wildtype hMeCP2 and Rett mutants with respect to their affinity for mC/mC; mean ± SEM.