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Stabilization of a nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator yields insight into disease-causing mutations

28 Jun 2017

Abstract excerpt

Characterization of the second nucleotide-binding domain (NBD2) of the cystic fibrosis transmembrane conductance regulator (CFTR) has lagged behind research into the NBD1 domain, in part because NBD1 contains the F508del mutation, which is the dominant cause of cystic fibrosis. Research on NBD2 has also been hampered by the overall instability of the domain and the difficulty of producing reagents. Nonetheless,...

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PMID: 28655774
DOI: 10.1074/jbc.m116.772335

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Stabilization of a nucleotide-binding domain of the cystic fibrosis transmembrane conductance regulator yields insight into disease-causing mutationsPMID 28655774Read ↗

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

Stability Prediction for Mutations in the Cytosolic Domains of 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 ↗

Nucleotide binding domains of human CFTR: a structural classification of critical residues and disease-causing mutations.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 ↗

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

Successful development and use of a thermodynamic stability screen for optimizing the yield of nucleotide binding domains.Semantic proximity Read ↗

Correcting mutant CFTR with a stabilizing nanobody reveals a novel active conformation of the channelSemantic proximity Read ↗

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

Disease-relevant mutations alter amino acid co-evolution networks in the second nucleotide binding domain of CFTR.Semantic proximity Read ↗

Structural Comparative Modeling of Multi-Domain F508del CFTR.Semantic proximity Read ↗

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