Membrane Binding Induces Distinct Structural Signatures in the Mouse Complexin-1C-Terminal Domain.

ABSTRACT: Complexins play a critical role in regulating SNARE-mediated exocytosis of synaptic vesicles. Evolutionary divergences in complexin function have complicated our understanding of the role these proteins play in inhibiting the spontaneous fusion of vesicles. Previous structural and functional characterizations of worm and mouse complexins have indicated the membrane curvature-sensing C-terminal domain of these proteins is responsible for differences in inhibitory function. We have characterized the structure and dynamics of the mCpx1 CTD in the absence and presence of membranes and membrane mimetics using NMR, ESR, and optical spectroscopies. In the absence of lipids, the mCpx1 CTD features a short helix near its N-terminus and is otherwise disordered. In the presence of micelles and small

SUBMITTER: Grasso EM 

PROVIDER: S-EPMC9794636 | biostudies-literature | 2023 Jan

REPOSITORIES: biostudies-literature