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. 2020 Jan 10;11:169. doi: 10.1038/s41467-019-13949-x

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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 Ribbon representations of the α3_SAM123/LAR-D1D2 complex structure. The two binding sites were highlighted by dashed boxes. b Surface representations showing the high conservation of the two binding sites. c, d Stereoview of the atomic details of the two binding sites between α3_SAM123 and LAR-D1D2, corresponding to the boxed regions shown in (a) with the same color. W856 in liprin-α3 and F1829 in LAR, indicated by asterisks, play the key role in the liprin-α3/LAR interaction. Hydrogen bonds and salt bridges are indicated by dashed lines. e Structural alignment of the SAM1 domains from the complex structures of α3_SAM123/LAR-D1D2, α2_SAM123/CASK_CaMK (PDB ID: 3TAC), and α2_SAM123/ β1_SAM123 (PDB ID: 3TAD) showing the orientation change of the αN-helix. f–h Analytical gel filtration analysis showing that either the W856Q mutation in liprin-α3 or the F1829 mutation in LAR disrupts the liprin-α3/LAR interaction. i ITC-based measurement of the binding of α3_SAM123 or its W856Q mutant to LAR_D1D2 and the binding of α3_SAM123 to the F1829E mutant of LAR_D1D2.