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Article

Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.

Protein science : a publication of the Protein Society - 1 Oct 2010

Wang Chi, Protasevich Irina, Yang Zhengrong, Seehausen Derek, Skalak Timothy, Zhao Xun, Atwell Shane, Spencer Emtage J, Wetmore Diana R, Brouillette Christie G, Hunt John F

Abstract excerpt

The lethal genetic disease cystic fibrosis is caused predominantly by in-frame deletion of phenylalanine 508 in the cystic fibrosis transmembrane conductance regulator (CFTR). F508 is located in the first nucleotide-binding domain (NBD1) of CFTR, which functions as an ATP-gated chloride channel on the cell surface. The F508del mutation blocks CFTR export to the surface due to aberrant retention in the endoplasmic...

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Identifiers

PMID: 20687163
DOI: 10.1002/pro.480
PMCID: PMC2998727

Genes

CFTR

Provenance

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.

Related research

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Integrated biophysical studies implicate partial unfolding of NBD1 of CFTR in the molecular pathogenesis of F508del cystic fibrosis.PMID 20687163Read ↗

Thermal unfolding studies show the disease causing F508del mutation in CFTR thermodynamically destabilizes nucleotide-binding domain 1.Semantic proximity Read ↗

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

ATP-dependent thermoring basis for the heat unfolding of the first nucleotide-binding domain isolated from human CFTRSemantic proximity Read ↗

Conformational Changes Relevant to Channel Activity and Folding within the first Nucleotide Binding Domain of the Cystic Fibrosis Transmembrane Conductance RegulatorSemantic proximity Read ↗

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

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

Structure and dynamics of NBD1 from CFTR characterized using crystallography and hydrogen/deuterium exchange mass spectrometry.Semantic proximity Read ↗

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

Correction of both NBD1 energetics and domain interface is required to restore 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 ↗

Dynamics intrinsic to cystic fibrosis transmembrane conductance regulator function and stability.Semantic proximity Read ↗

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