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. 2023 Dec 4;4:46. doi: 10.1186/s43556-023-00156-w

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© The Author(s) 2023

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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Fig. 6 — Conformational alterations during Class F receptor activation. Class F receptors are composed of a cystine-rich domain (CRD), linker domain (LD) and transmembrane domain (TMD), and the inactive state is shown on the left. When activated by the ligand, TM6 in SMO and FZDs undergoes an outward shift, and a hydrogen bond between the conserved residues R^6.32 and W^7.55 in the inactive receptor is disrupted. The difference between SMO and FZDs is that the TM6 in SMO exhibits a parallel outward shift, while FZDs achieve a similar displacement of its cytoplasmic segment through a helical kink. This difference may be caused by the conserved residue P^6.43 in the FZDs (as opposed to F^6.43 in SMO). PDB ID of these structures: active mSMO (6O3C), inactive hSMO (5I7D); active FZD7 (7EVW), inactive FZD5 (6WW2)