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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. 4 — a The D1/D1 interaction found between the four LAR-D1D2 protomers in one asymmetric unit. b Stereoview of the atomic details for one LAR-D1D2 packing interface boxed in (a). The other two D1/D1 packing interfaces were shown in Supplementary Fig. 9a. Hydrogen bonds and salt bridges were indicated by dashed lines. Residues (R1415, Q1417, and N1418) mutated to alanine in the RQN mutation of LAR were indicated by asterisks in the right panel. c COS7 cells co-transfected with GFP-liprin-α1 and wild-type LAR-Flag or its RQN mutant. Regions of interest were highlighted by yellow boxes and enlarged four times on the right of each merged image. Scale bar, 10 μm. d Analytical gel filtration analysis showing the oligomer formation induced by the L1539C/T1593C double-cysteine mutation in LAR_D1D2. e Molecular weight measurement of different oligomeric fractions of the double-cysteine mutant by using multiangle static light scattering. The theoretical molecular weight of LAR_D1D2 is 65.9 kDa.