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Article

The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain.

PloS one - 30 Nov 2010

Hoelen Hanneke, Kleizen Bertrand, Schmidt Andre, Richardson John, Charitou Paraskevi, Thomas Philip J, Braakman Ineke

Abstract excerpt

In the vast majority of cystic fibrosis (CF) patients, deletion of residue F508 from CFTR is the cause of disease. F508 resides in the first nucleotide binding domain (NBD1) and its absence leads to CFTR misfolding and degradation. We show here that the primary folding defect arises during synthesis, as soon as NBD1 is translated. Introduction of either the I539T or G550E suppressor mutation in NBD1 partially...

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Source

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Identifiers

PMID: 21152102
DOI: 10.1371/journal.pone.0015458
PMCID: PMC2994901

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

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The primary folding defect and rescue of ΔF508 CFTR emerge during translation of the mutant domain.PMID 21152102Read ↗

Cystic fibrosis: a disease of altered protein folding.Semantic proximity Read ↗

CFTR trafficking mutations disrupt cotranslational protein folding by targeting biosynthetic intermediates.Semantic proximity Read ↗

Diminished self-chaperoning activity of the DeltaF508 mutant of CFTR results in protein misfolding.Semantic proximity Read ↗

The cystic fibrosis-causing mutation deltaF508 affects multiple steps in cystic fibrosis transmembrane conductance regulator biogenesis.Semantic proximity Read ↗

Alteration of the Cystic Fibrosis Transmembrane Conductance Regulator Folding PathwaySemantic proximity Read ↗

Mutations in the nucleotide binding domain 1 signature motif region rescue processing and functional defects of cystic fibrosis transmembrane conductance regulator delta f508.Semantic proximity Read ↗

ABC-transporter CFTR folds with high fidelity through a modular, stepwise pathwaySemantic proximity Read ↗

Impact of the ΔF508 Mutation in First Nucleotide-binding Domain of Human Cystic Fibrosis Transmembrane Conductance Regulator on Domain Folding and StructureSemantic proximity Read ↗

Cystic fibrosis mutations lead to carboxyl-terminal fragments that highlight an early biogenesis step of the cystic fibrosis transmembrane conductance regulator.Semantic proximity Read ↗

Structure basis of CFTR folding, function and pharmacology.Semantic proximity Read ↗

Structural stability of purified human CFTR is systematically improved by mutations in nucleotide binding domain 1.Semantic proximity Read ↗

Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.Semantic proximity Read ↗

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