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Avidity within the N-terminal anchor drives α-synuclein membrane interaction and insertion

Ersoy Cholak1, Katrine Bugge2, Adree Khondker3

  • 1Department of Drug Design and Pharmacology, University of Copenhagen, Copenhagen, Denmark.

FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology
|April 12, 2020
PubMed
Summary

Alpha-synuclein (aSN) membrane binding requires dual interactions: N-terminal tail insertion and helix formation. This avidity is crucial for aSN

Keywords:
IDPN-acetylationNMRXRDaSNaviditymembrane interactionα-synuclein

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