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 journalArticleAcademicpeer-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 languageUndefined
Pages (from-to)7796-7797
Number of pages2
JournalJournal of the American Chemical Society
Volume130
Issue number25
DOIs
Publication statusPublished - 2008

Keywords

  • METIS-248978
  • IR-75522

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