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J Cyst Fibros. 2008 Jul;7(4):295-300. doi: 10.1016/j.jcf.2007.11.008. Epub 2008 Jan 29.

DeltaF508 mutation increases conformational flexibility of CFTR protein.

Author information

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

Abstract

BACKGROUND:

The deletion of Phe508 in the first nucleotide-binding domain of the CFTR protein is the most common mutation leading to cystic fibrosis.

METHODS:

We present a Molecular Dynamics study on the native and mutated domains, based on their recently published crystal structure.

RESULTS:

DeltaF508 CFTR has much more conformational freedom compared to the wild-type, and exposes its hydrophobic interior to the solution.

CONCLUSIONS:

The increased flexibility might be the reason for the recognition of mutated CFTR by the housekeeping proteins and its premature degradation. This, in turn results in reduction of population of functional channels at the epithelial cell surface and disease phenotype.

PMID:
18234567
DOI:
10.1016/j.jcf.2007.11.008
[PubMed - indexed for MEDLINE]
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