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

Malte Drescher; Gertjan Veldhuis; Bart D van Rooijen; Sergey Milikisyants; Vinod Subramaniam; Martina Huber

doi:10.1021/ja801594s

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

Malte Drescher, Gertjan Veldhuis, Bart D van Rooijen, Sergey Milikisyants, Vinod Subramaniam, Martina Huber

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

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.

Original language	English
Pages (from-to)	7796-7
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 - 25 Jun 2008

Keywords

Magnetic Resonance Spectroscopy
Models, Molecular
Protein Binding
Protein Structure, Secondary
Transport Vesicles
alpha-Synuclein
Journal Article
Research Support, Non-U.S. Gov't

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

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.",

keywords = "Magnetic Resonance Spectroscopy, Models, Molecular, Protein Binding, Protein Structure, Secondary, Transport Vesicles, alpha-Synuclein, Journal Article, Research Support, Non-U.S. Gov't",

author = "Malte Drescher and Gertjan Veldhuis and {van Rooijen}, {Bart D} and Sergey Milikisyants and Vinod Subramaniam and Martina Huber",

year = "2008",

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AU - Drescher, Malte

AU - Veldhuis, Gertjan

AU - van Rooijen, Bart D

AU - Milikisyants, Sergey

AU - Subramaniam, Vinod

AU - Huber, Martina

PY - 2008/6/25

Y1 - 2008/6/25

N2 - 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.

AB - 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.

KW - Magnetic Resonance Spectroscopy

KW - Models, Molecular

KW - Protein Binding

KW - Protein Structure, Secondary

KW - Transport Vesicles

KW - alpha-Synuclein

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

U2 - 10.1021/ja801594s

DO - 10.1021/ja801594s

M3 - Article

C2 - 18512917

SN - 0002-7863

VL - 130

SP - 7796

EP - 7797

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 25

ER -

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

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Keywords

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