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Article

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

Cell - 20 Jan 2012

Rabeh Wael M, Bossard Florian, Xu Haijin, Okiyoneda Tsukasa, Bagdany Miklos, Mulvihill Cory M, Du Kai, di Bernardo Salvatore, Liu Yuhong, Konermann Lars, Roldan Ariel, Lukacs Gergely L

Abstract excerpt

The folding and misfolding mechanism of multidomain proteins remains poorly understood. Although thermodynamic instability of the first nucleotide-binding domain (NBD1) of ΔF508 CFTR (cystic fibrosis transmembrane conductance regulator) partly accounts for the mutant channel degradation in the endoplasmic reticulum and is considered as a drug target in cystic fibrosis, the link between NBD1 and CFTR misfolding...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22265408
DOI: 10.1016/j.cell.2011.11.024
PMCID: PMC3431169

Genes

CFTR

Provenance

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Correction of both NBD1 energetics and domain interface is required to restore ΔF508 CFTR folding and function.PMID 22265408Read ↗

Mechanism-based corrector combination restores ΔF508-CFTR folding and function.Semantic proximity Read ↗

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

CFTR misfolds during native-centric simulations due to entropic penalties of native state formationSemantic proximity Read ↗

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

Alteration of the Cystic Fibrosis Transmembrane Conductance Regulator Folding 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: a disease of altered protein folding.Semantic proximity Read ↗

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

Pharmacological chaperones improve intra-domain stability and inter-domain assembly via distinct binding sites to rescue misfolded CFTR.Semantic proximity Read ↗

Folding correctors can restore CFTR posttranslational folding landscape by allosteric domain-domain coupling.Semantic proximity Read ↗

A Topological Switch in the Cystic Fibrosis Transmembrane Conductance Regulator Modulates Channel Activity and Sensitivity to Disease-Causing MutationSemantic proximity Read ↗

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

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