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Article

Ligand binding to a remote site thermodynamically corrects the F508del mutation in the human cystic fibrosis transmembrane conductance regulator.

The Journal of biological chemistry - 16 Nov 2018

Wang Chi, Aleksandrov Andrei A, Yang Zhengrong, Forouhar Farhad, Proctor Elizabeth A, Kota Pradeep, An Jianli, Kaplan Anna, Khazanov Netaly, Boël Grégory, Stockwell Brent R, Senderowitz Hanoch, Dokholyan Nikolay V, Riordan John R, Brouillette Christie G, Hunt John F

Abstract excerpt

Many disease-causing mutations impair protein stability. Here, we explore a thermodynamic strategy to correct the disease-causing F508del mutation in the human cystic fibrosis transmembrane conductance regulator (hCFTR). F508del destabilizes nucleotide-binding domain 1 (hNBD1) in hCFTR relative to an aggregation-prone intermediate. We developed a fluorescence self-quenching assay for compounds that prevent...

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Identifiers

PMID: 29903914
DOI: 10.1074/jbc.RA117.000819
PMCID: PMC6240863

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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