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ID: 233392.0, MPI für biophysikalische Chemie / Molekulare Biologie (Dr. Thomas M. Jovin)
Familial mutants of α-synuclein with increased neurotoxicity have a destabilized conformation
Authors:Bertoncini, C. W.; Fernandez, C. O.; Griesinger, C.; Jovin, T. M.; Zweckstetter, M.
Language:English
Date of Publication (YYYY-MM-DD):2005-09-02
Title of Journal:Journal of Biological Chemistry
Volume:280
Start Page:30649
End Page:30652
Review Status:Peer-review
Audience:Not Specified
Intended Educational Use:No
Abstract / Description: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.
Free Keywords:none available
Last Change of the Resource (YYYY-MM-DD):2005-08-29
External Publication Status:published
Document Type:Article
Communicated by:N. N.
Affiliations:MPI für biophysikalische Chemie/Abt. Thomas Jovin / 060
MPI für biophysikalische Chemie/Abt. Christian Griesinger / 030
MPI für biophysikalische Chemie/AG Markus Zweckstetter
External Affiliations:Instituto de Biología Molecular y Celular de Rosario, Consejo Nacional de Investigaciones Científicas y Técnicas, Universidad Nacional de Rosario, Suipacha 531, S2002LRK, Rosario, Argentina
Identifiers:URL:http://www.jbc.org/cgi/content/full/280/35/30649?m...
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