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Cystic Fibrosis Development Better Understood
According to a report in the open-access journal PLoS
Computational Biology, there is a specific molecular
mechanism that could be responsible for the development of cystic
fibrosis. The University of North Carolina at Chapel Hill researchers
suggest better understanding of the disease may help to develop new
corrective treatments.
About 1 in 3000 children is born with cystic fibrosis (CF) in the US
every year. It is a fatal disease that is caused by a defective gene
that produces a misshapen form of a protein called the cystic fibrosis
transmembrane conductance regulator (CFTR). Because their bodies
rapidly remove the mutant protein, people afflicted with CF do not have
the necessary amount of CFTR for proper cellular functions.
Specifically, protein deletion happens in a major domain of CFTR called
NBD1. Previous experimental research suggests that the mutant NBD1 is
more likely to misfold than normal NBD1, and the result is premature
degradation of CFTR.
Team leader Nikolay Dokholyan reports that the molecular basis in CF of
the increased tendency to misfold has been unknown. "Understanding
molecular etiology of the disease is a key step to developing
pharmaceutical strategies to fight this disease," notes Dokholyan.
The researchers used molecular dynamics simulations, which consisted of
analyzing several simulations of how normal and mutant NBD1 folded.
This is much like a virtual experiment, with atoms and molecules being
permitted to change according to known physical laws. The virtual
experiment lets researchers see how atoms actually move. Analyzing the
NBD1 protein, the simulations demonstrated that the mutant NBD1 causes
CF tends to misfold with greater frequency.
Further, the researchers could identify important pairs of amino acid
residues that must come together in order for NBD1 to correctly fold.
They identified the residues by analyzing the structures of normal and
mutant NBD1 domains. Since the interactions are modulators of CFTR
folding, they are potential modulators of CF.
"Computer simulations approximate our understanding of natural
phenomena. That our simulations correlated with known experimental
studies is remarkable," Dokholyan said. "More importantly, the
molecular details of aberrant NBD1 folding provides guidance for the
design of small molecule drugs to correct the most prevalent and
pathogenic mutation in CFTR."
Diminished Self-Chaperoning Activity of the DF508 Mutant of
CFTR Results in Protein Misfolding
Serohijos AWR, Hegedűs T, Riordan JR, Dokholyan NV
PLoS Computational Biology (2008).
4(2): e1000008.
doi:10.1371/journal.pcbi.1000008
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About PLoS Computational Biology
PLoS Computational Biology
(www.ploscompbiol.org)
features works of exceptional significance that
further our understanding of living systems at all scales through the
application of computational methods. All works published in PLoS
Computational Biology are open access. Everything is immediately
available subject only to the condition that the original authorship
and source are properly attributed. Copyright is retained by the
authors. The Public Library of Science uses the Creative Commons
Attribution License.
About the Public Library of Science
The Public Library of Science (PLoS) is a non-profit organization
of scientists and physicians committed to making the world's
scientific and medical literature a freely available public resource.
For more information, visit http://www.plos.org
Written by: Peter M Crosta
Copyright: Start Sanatate
Not to be reproduced without permission of Start Sanatate
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