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. 2021 Mar 25;11:6842. doi: 10.1038/s41598-021-83240-x

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© The Author(s) 2021, corrected publication 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 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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c407 interaction with the 3D structure of the F508del-CFTR MSDs:NBDs assembly. (A) Ribbon representation of the 3D structure model of the F508del-CFTR MSDs:NBDs assembly. NBD1 is colored in blue, MSD2 in brown red. The box highlights the position on this assembly of the putative c407 binding site, which is detailed in the right part of the figure. (B) Predicted c407 binding site in the context of the isolated F508del-NBD1 (extracted from the whole MSDs:NBDs architecture). In the inset is represented superimposition with the 3D structure of F508del MSDs:NBDs assembly, in order to highlight the similar position of the c407 (pink) external phenyl ring and ICL4 F1068 (red brown). (C) Predicted c407 binding site in the context of the F508del MSD:NBD assembly (same orientation as in Panel B). In the inset is represented the superimposition with the 3D structure of WT NBD1, in order to highlight the similar position of the c407 (green) external phenyl ring and F508 (blue). (D) Extended c407 analog, G1, is shown with the extension designed to interact with Y1073, thereby adding contacts with ICL4.