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. 2025 Jul 30;5(4):593–601. doi: 10.1021/acsbiomedchemau.5c00014

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© 2025 The Author. Published by American Chemical Society

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Cooperative and protective folding pathways of NBD1 in hCFTR in response to modulators. Cryo-EM structures of activated phosphorylated hCFTR/E1371Q with Mg/ATP/VX770 bound (PDB: 6O2P) and open phosphorylated hCFTR/ΔF508/E1371Q with Mg/ATP/VX809/VX445 bound (PDB: 8EIO) are used for the models. VX770, VX-445, and VX-809 are colored green. The N-terminal, α- and β-subdomains in NBD1 are colored orange, cyan, and blue, respectively. The biggest thermorings in NBD1 are shown in red. The residues responsible for the least-stable noncovalent interactions in NBD1 are shown in space fills.