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. 2022 Sep 27;32(11):982–994. doi: 10.1038/s41422-022-00725-8

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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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/..

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Fig. 3 — a Overall structure of WTAP homodimer. The distortion angles of the axes of coiled-coils at L1, L2, and L3 are shown in the left, upper, and right panels, respectively. The axes of coiled-coils are shown as black lines in each panel. b, c Two different views of the WTAP homodimer surface colored by electrostatic potential (b) and sequence conservation (c). d Intermolecular contacts between WTAP-a and WTAP-b around L2/L2’, corresponding to the green box in b and c. e Sequence alignment of the WTAP homodimer (138–163) containing the L2/L2’ region. Hs, Homo sapiens; Dr, Danio rerio; Xl, Xenopus laevis; Dm, Drosophila melanogaster; At, Arabidopsis thaliana. The secondary structure depictions of WTAP-a and WTAP-b are shown in the top and bottom panels. Conserved and similar residues are boxed with red ground and red font, respectively. f Intermolecular contacts between WTAP-a and WTAP-b around L3/L3’, corresponding to the orange box in b and c. g Sequence alignment of the WTAP homodimer (160–185) containing the L3/L3’ region, marked as e.