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- Title
Arrest of CFTR?F508 folding.
- Authors
Cyr, Douglas M.
- Abstract
This article discusses diseases caused due to deletion of residue 508 in CFTR. Many diseases result from mutant proteins that either fold slowly and are degraded prematurely, or are dynamically unstable and assume toxic folds. To deal with such rogue conformers inside the cell, the protein quality control system in the endoplasmic reticulum suppresses aggregation and promotes degradation by the proteasome. The molecular chaperone Hsc70 is one factor in this system. Cystic fibrosis (CF) is caused by the misfolding and premature degradation of CFTR mutants, the most prevalent of which in the population is the deletion of Phe508.
- Subjects
MOLECULAR chaperones; CYSTIC fibrosis; GENETIC disorders; PROTEINS; BIOMOLECULES; CYTOCHEMISTRY
- Publication
Nature Structural & Molecular Biology, 2005, Vol 12, Issue 1, p2
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb0105-2