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. 2017 Sep 21;7:12050. doi: 10.1038/s41598-017-11416-5

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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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Structure of the O-GlcNAcylated Cx40 and Cx43 proteins and their electrostatic potential surface. (a) The side view of Cx40 structure with O-GlcNAcylation at the residue Serine 18. (b) The top view of Cx40 with O-GlcNAcylation. (c,d) The electrostatic potential surface of Cx40 and Cx43 with O-GlcNAcylation. The O-GlcNAc on the surface is highlighted with dotted circles. Electrostatic potential surfaces are blue for positive, white for hydrophobic, and red for negative. All images were generated by the PyMOL (Available: http://www.pymol.org).