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PMID: 18512917 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein.

Journal of the American Chemical Society ·Vol. 130 ·No. 25 ·2008-06-25 ·Pages 7796-7

Drescher M, Veldhuis G, van Rooijen BD, Milikisyants S, Subramaniam V, Huber M

Abstract

alpha-Synuclein (alphaS) is the main component of Lewy bodies from Parkinson's disease. That alphaS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of alphaS sheds light on the most likely structure. For alphaS bound to vesicles large enough to accommodate also the extended conformation, an antiparallel helix conformation is found. This suggests that the bent structure shown is the preferred conformation of alphaS on membranes.

MeSH Terms
Magnetic Resonance Spectroscopy Models, Molecular Protein Binding Protein Structure, Secondary Transport Vesicles/chemistry,metabolism alpha-Synuclein/chemistry,metabolism
Chemicals
alpha-Synuclein
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Drescher Malte
Department of Molecular Physics, Leiden University, P.O. Box 9504, 2300 RA Leiden, The Netherlands.
Veldhuis Gertjan
van Rooijen Bart D
Milikisyants Sergey
Subramaniam Vinod
Huber Martina
Article Info
Journal
Journal of the American Chemical Society
Abbr.
J Am Chem Soc
ISSN
1520-5126
Published
2008-06-25
Epub
2008-00-31
Pages
7796-7
Language
English
Region
United States
NLM ID
7503056
Subset
IM
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