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. 2019 Jan 24;9:600. doi: 10.1038/s41598-018-37306-y

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© The Author(s) 2019

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 Influenza D nucleoprotein. (a) Structure of the tetrameric D/NP, with 3 protomers shown in surface (respectively in green, pink and cyan) and the fourth in cartoon (deep purple). (b) Cartoon representation of one monomer of D/NP with the α-helixes in deep purple and β-strands in yellow. (c) Detail of the interactions between two protomers of the tetrameric D/NP as shown in (a). The conserved R425 of one protomer (shown as deep purple cartoon) stabilized the position of the oligomerization loop at the surface of the neighbouring protomer, through its conserved E352. (d) Sequence alignment of the salt bridges of the oligomerization-loop of one protomer to the NP_CORE of the neighbour protomers. For the sequences see Table 1.