A broken α-helix in folded α-synuclein

Sreeganga Chandra, Xiaocheng Chen, Jose Rizo-Rey, Reinhard Jahn, Thomas C. Südhof

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Abstract

α-Synuclein is a small cytosolic protein of presynaptic nerve terminals composed of seven 11-residue repeats and a hydrophilic tail. α-Synuclein misfolding and dysfunction may contribute to the pathogenesis of Parkinson's disease and neurodegenerative dementias, but its normal folding and function are unknown. In solution, α-synuclein is natively unstructured but assumes an α-helical conformation upon binding to phospholipid membranes. We now show that this conformation of α-synuclein consists of two α-helical regions that are interrupted by a short break. The structural organization of the α-helices of α-synuclein was not anticipated by sequence analyses and may be important for its pathogenic role.

Original languageEnglish (US)
Pages (from-to)15313-15318
Number of pages6
JournalJournal of Biological Chemistry
Volume278
Issue number17
DOIs
Publication statusPublished - Apr 25 2003

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ASJC Scopus subject areas

  • Biochemistry

Cite this

Chandra, S., Chen, X., Rizo-Rey, J., Jahn, R., & Südhof, T. C. (2003). A broken α-helix in folded α-synuclein. Journal of Biological Chemistry, 278(17), 15313-15318. https://doi.org/10.1074/jbc.M213128200