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. 2022 Nov 9;12:19089. doi: 10.1038/s41598-022-23342-2

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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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(A) Post-fusion six-helix bundle (PDB ID: 6LXT) illustrating the location of the N1192S mutation. S1192 is rendered as a CPK residue (one per receptor monomer) and color-coded by atom type as described in Fig. 5. (B) Detailed view of side chain packing interactions formed by N1192. K933 is from the neighboring monomer; this image illustrates the tight packing contacts formed by proximate side chains that stabilize the six-helix bundle fusion structure. C) Detailed view of side chain packing interactions formed by the S1192 mutant. The helix bundle orientation is identical to that in Fig. 7B.