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  Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation

Bertoncini, C. W., Fernandez, C. O., Griesinger, C., Jovin, T. M., & Zweckstetter, M. (2005). Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation. Journal of Biological Chemistry, 280, 30649-30652. Retrieved from http://www.jbc.org/cgi/content/full/280/35/30649?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&andorexactfulltext=and&searchid=1&FIRSTINDEX=0&sortspec=relevance&volume=280&firstpage=30649&resourcetype=HWCIT.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0012-E826-D Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-E098-3
Genre: Journal Article

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 Creators:
Bertoncini, C. W.1, Author              
Fernandez, C. O.2, Author              
Griesinger, C.2, Author              
Jovin, T. M.1, Author              
Zweckstetter, M.3, Author              
Affiliations:
1Department of Molecular Biology, MPI for biophysical chemistry, Max Planck Society, ou_578628              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              
3Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              

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 Abstract: A30P and A53T mutations of the presynaptic protein α-synuclein are associated with familial forms of Parkinson’s disease. NMR spectroscopy demonstrates that Parkinsonism-linked mutations greatly perturb specific tertiary interactions essential for the native state of α-synuclein. However, α-synuclein is not completely unfolded, but exhibits structural fluctuations on the time scale of secondary structure formation, and loses its native conformation gradually when protein stability decreases. The redistribution of the ensemble of α-synuclein conformers may underlie toxic gain-of-function by fostering self-association and altered binding affinity to ligands and receptors.

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Language(s): eng - English
 Dates: 2005-08-292005-09-02
 Publication Status: Published in print
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 Rev. Method: Peer
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 280 Sequence Number: - Start / End Page: 30649 - 30652 Identifier: -