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. 2021 May 19;12:2956. doi: 10.1038/s41467-021-23254-1

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© The Author(s) 2021

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 Comparison of domains DBL2, DBL3 and DBL4. The red loop shows the “WIW-motif”-loop from each domain, the green α-helix shows HB1. In DBL2, an additional loop in HB1 introduces a kink in the α-helix. b DBL2 domain shown as cartoon, the red loop shows S1 (HB4 and “WIW-motif”-loop), blue α-helices show S2 (HB3-HB5) and green α-helices show S3 (HB2-HB1). S1-S3 residue boundaries and colors are shown in legend below. The distal nitrogen atom of Lys/Arg residues side chains in binding groove are shown as blue spheres and labeled according to residue number. c Structural details of the interaction between “WIW-motif” and HB2/HB3 in DBL2. Interacting side chains are shown as sticks and are labeled with residue numbers. d LOGO conservation analyses of “WIW-motif”-loop AA553-583 in var2csa variants. Residue number from VAR2CSA sequence shown below.