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

Malte Drescher; G.J. Veldhuis; G. Veldhuis; Bart van Rooijen; Sergey Milikisyants; Vinod Subramaniam; Martina Huber

doi:10.1021/ja801594s

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

Malte Drescher, G.J. Veldhuis, G. Veldhuis, Bart van Rooijen, Sergey Milikisyants, Vinod Subramaniam, Martina Huber

Research output: Contribution to journal › Article › Academic › peer-review

88 Citations (Scopus)

Abstract

α-Synuclein (αS) is the main component of Lewy bodies from Parkinson’s disease. That αS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of αS sheds light on the most likely structure. For αS 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 αS on membranes.

Original language	Undefined
Pages (from-to)	7796-7797
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	130
Issue number	25
DOIs	https://doi.org/10.1021/ja801594s
Publication status	Published - 2008

Keywords

METIS-248978
IR-75522

Access to Document

10.1021/ja801594s

Cite this

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title = "Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein",

abstract = "α-Synuclein (αS) is the main component of Lewy bodies from Parkinson{\textquoteright}s disease. That αS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of αS sheds light on the most likely structure. For αS 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 αS on membranes.",

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author = "Malte Drescher and G.J. Veldhuis and G. Veldhuis and {van Rooijen}, Bart and Sergey Milikisyants and Vinod Subramaniam and Martina Huber",

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AU - Drescher, Malte

AU - Veldhuis, G.J.

AU - Veldhuis, G.

AU - van Rooijen, Bart

AU - Milikisyants, Sergey

AU - Subramaniam, Vinod

AU - Huber, Martina

PY - 2008

Y1 - 2008

N2 - α-Synuclein (αS) is the main component of Lewy bodies from Parkinson’s disease. That αS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of αS sheds light on the most likely structure. For αS 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 αS on membranes.

AB - α-Synuclein (αS) is the main component of Lewy bodies from Parkinson’s disease. That αS binds to membranes is known, but the conformation it adopts is still unclear. Pulsed EPR on doubly spin-labeled variants of αS sheds light on the most likely structure. For αS 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 αS on membranes.

KW - METIS-248978

KW - IR-75522

U2 - 10.1021/ja801594s

DO - 10.1021/ja801594s

M3 - Article

VL - 130

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EP - 7797

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

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