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. 2024 Aug 31;15:7574. doi: 10.1038/s41467-024-52045-7

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© The Author(s) 2024

Open Access This article is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License, which permits any non-commercial use, sharing, 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 you modified the licensed material. You do not have permission under this licence to share adapted material derived from this article or parts of it. 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-nc-nd/4.0/.

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Fig. 2 — a,b Cryo-EM map (left) and model (right) of CCR6 complex with anti-BRIL Fab and anti-Fab Nb bound to a OXM1 (orange carbon spheres) and SQA1 (yellow carbon spheres), or b OXM2 (slate carbon spheres) and SQA1 (yellow carbon spheres). Protein is coloured by subunit as follows: Fab heavy chain, magenta; Fab light chain, salmon; Nb, yellow; CCR6, aquamarine in a and deep teal in b. c Extracellular (EC) view of CCR6 bound to OXM analogues, OXM1 (left) and OXM2 (right). d Intracellular (IC) view of CCR6 bound to the SQA analogue, SQA1. Both c and d use the same colour code as a and b. e SQA1, OXM1, and f SQA1, OXM2 fits into the cryo-EM density maps of the two structures from two viewing angles.