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. 2021 Dec 9;12:7171. doi: 10.1038/s41467-021-27475-2

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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. 3 — a, b Comparison of the apo HHIP-N structure (a) and HHIP-N:SOS complex. Colour coding is as in Fig. 1b. For HHIP-N:apo, the disordered GAG-binding domain is shown as a dashed line. In the HHIP-N:SOS complex three SOS molecules interact with the GAG-binding domain. c Electrostatic surface potential of the HHIP-N:SOS complex, displayed from −10 kT/e to +10 kT/e. d Close-up view of HHIP-N:SOS binding site showing the region marked in C. Hydrogen bonds are shown as dashed lines (c, d rotated 90^° around the x-axis relative to B). Mutations previously observed to decrease GAG-binding affinity and cause dysfunction of HHIP are marked with asterisks²⁸. e Heparin affinity chromatography of different HHIP constructs eluted from a linear gradient of NaCl from 20 to 1000 mM (green line). Traces corresponding to different constructs are coloured according to the accompanying legend (inset).