Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

Binsen Li; Peng Ge; Kevin A. Murray; Phorum Sheth; Meng Zhang; Gayatri Nair; Michael R. Sawaya; Woo Shik Shin; David R. Boyer; Shulin Ye; David S. Eisenberg; Z. Hong Zhou; Lin Jiang

doi:10.1038/s41467-018-05971-2

Nature Communications (Sep 2018)

Cryo-EM of full-length α-synuclein reveals fibril polymorphs with a common structural kernel

Binsen Li,
Peng Ge,
Kevin A. Murray,
Phorum Sheth,
Meng Zhang,
Gayatri Nair,
Michael R. Sawaya,
Woo Shik Shin,
David R. Boyer,
Shulin Ye,
David S. Eisenberg,
Z. Hong Zhou,
Lin Jiang

Affiliations

Binsen Li: Department of Neurology, David Geffen School of Medicine, UCLA
Peng Ge: California Nano Systems Institute, UCLA
Kevin A. Murray: Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA
Phorum Sheth: Department of Neurology, David Geffen School of Medicine, UCLA
Meng Zhang: Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA
Gayatri Nair: Department of Neurology, David Geffen School of Medicine, UCLA
Michael R. Sawaya: Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA
Woo Shik Shin: Department of Neurology, David Geffen School of Medicine, UCLA
David R. Boyer: Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA
Shulin Ye: California Nano Systems Institute, UCLA
David S. Eisenberg: Departments of Biological Chemistry and Chemistry and Biochemistry, Howard Hughes Medical Institute, UCLA-DOE Institute, UCLA
Z. Hong Zhou: California Nano Systems Institute, UCLA
Lin Jiang: Department of Neurology, David Geffen School of Medicine, UCLA

DOI: https://doi.org/10.1038/s41467-018-05971-2
Journal volume & issue: Vol. 9, no. 1
pp. 1 – 10

Abstract

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The intrinsically disordered protein alpha-synuclein (aSyn) forms polymorphic fibrils. Here the authors provide molecular insights into aSyn fibril polymorphism and present the cryo-EM structures of the two predominant species, a rod and a twister both determined at 3.7 Å resolution.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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