Antiparallel arrangement of the helices of vesicle-bound alpha-synuclein.
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.
Drescher
Malte
M
Department of Molecular Physics, Leiden University, P.O. Box 9504, 2300 RA Leiden, The Netherlands.
Veldhuis
Gertjan
G
van Rooijen
Bart D
BD
Milikisyants
Sergey
S
Subramaniam
Vinod
V
Huber
Martina
M
D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D022161:Transport Vesicles / Q000737:chemistry* / Q000378:metabolism; D051844:alpha-Synuclein / Q000737:chemistry* / Q000378:metabolism
D051844:alpha-Synuclein