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. 2020 May 19;9(5):53. doi: 10.1038/s41389-020-0235-y

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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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Fig. 2 — a FBW7 WD40 domain. Ribbon diagram of the 8 WD-repeats in FBW7 WD40. Tryptophan-aspartic acid (WD) dipeptides are depicted as spheres. b Inter-residue interactions in MCV sT and WD40 domain docking models. To select and interpret correlated mutations in the WD40, MCV sT (cyan)-WD40 (green) complex structures from 4 potential docking models were analyzed and visualized based on the use of inter-residue contacts (green spears) with amino acids LK (red spears) in LSD. c WD8 blade beta propeller is a critical site for both sT and LT interactions. Co-immunoprecipitation assay shows that both MCV LT and sT binding were reduced by FBW7-WD40 mutations in residues V375 and K377 (V375A/K377N). This mutation is located within the WD8 blade.