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. 2022 Apr 27;13:2269. doi: 10.1038/s41467-022-29927-9

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© The Author(s) 2022

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. 1 — A Crystal structure of two copies of VP35’s IID (dark gray and light blue) bound to dsRNA (light gray) via two flat interfaces (PDB ID 3L25). Mutations to residues highlighted in pink and yellow sticks eliminate dsRNA binding. B Isolated chain B from the same view as panel A and after 90° rotation in the Y axis now highlighting the dsRNA interacting VP35 surface in the blunt-end-binding protomer. The blunt-end-binding interface (pink, 3L25 chain B) is shown as spheres to highlight that VP35 lacks deep pockets amenable to binding small molecules.