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Related Concept Videos

Cystic Fibrosis: Pathogenesis01:23

Cystic Fibrosis: Pathogenesis

Cystic fibrosis (CF), an autosomal recessive disorder, significantly affects the function of exocrine glands. This genetically inherited disease is characterized by the production of thick and sticky mucus, which can severely affect various organs and systems in the body.
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Cystic Fibrosis: Management01:24

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Cystic fibrosis (CF) is an autosomal recessive disorder that predominantly affects individuals of Northern European descent, occurring at a rate of 1 in 3500. It is caused by a genetic mutation in a gene on chromosome 7, most commonly the ΔF508 mutation, that codes for the cystic fibrosis transmembrane conductance regulator (CFTR) protein. This results in thicker mucus secretions and obstruction pathologies in multiple organs, including the lungs and sinuses.
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Updated: Jul 7, 2026

Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
08:59

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Published on: February 12, 2019

DeltaF508 mutation increases conformational flexibility of CFTR protein.

G Wieczorek1, P Zielenkiewicz2

  • 1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawinskiego 5a, 02-106 Warszawa, Poland.

Journal of Cystic Fibrosis : Official Journal of the European Cystic Fibrosis Society
|February 1, 2008
PubMed
Summary

The most common cystic fibrosis mutation, DeltaF508 CFTR, exhibits increased flexibility, exposing its interior. This conformational change may lead to protein degradation and the disease phenotype.

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08:59

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Forskolin-induced Swelling in Intestinal Organoids: An In Vitro Assay for Assessing Drug Response in Cystic Fibrosis Patients
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Published on: February 11, 2017

Area of Science:

  • Biochemistry
  • Structural Biology
  • Molecular Biophysics

Background:

  • Cystic fibrosis is primarily caused by the DeltaF508 mutation in the CFTR protein's nucleotide-binding domain.
  • This mutation involves the deletion of phenylalanine at position 508.

Purpose of the Study:

  • To investigate the structural and dynamic differences between wild-type and DeltaF508 CFTR.
  • To elucidate the molecular mechanisms underlying DeltaF508 CFTR dysfunction.

Main Methods:

  • Molecular Dynamics simulations were employed.
  • The study utilized the recently published crystal structure of the CFTR domains.

Main Results:

  • DeltaF508 CFTR displays significantly greater conformational freedom than wild-type CFTR.
  • The mutated protein exposes its hydrophobic interior to the surrounding solution.

Conclusions:

  • Increased flexibility of DeltaF508 CFTR may facilitate recognition by cellular "housekeeping" proteins.
  • This interaction potentially leads to premature degradation of the mutant protein.
  • Reduced levels of functional CFTR channels at the cell surface contribute to the cystic fibrosis disease phenotype.