Title: Stabilization of vimentin coil2 fragment via an engineered disulfide
Authors: Chernyatina, Anastasia
Strelkov, Sergei # ×
Issue Date: Jan-2012
Publisher: Academic Press
Series Title: Journal of Structural Biology vol:177 issue:1 pages:46-53
Abstract: Cytoskeletal intermediate filaments (IFs) assemble from the elementary dimers based on a segmented α-helical coiled-coil (CC) structure. Crystallographic studies of IF protein fragments remain the main route to access their atomic structure. To enable crystallization, such fragments must be sufficiently short. As a consequence, they often fail to assemble into the correct CC dimers. In particular, human vimentin fragment D3 corresponding to the first half of coil2 (residues 261-335) stays monomeric in solution. We have induced its dimerization via introducing a disulfide link between two cysteines engineered in the hydrophobic core of the CC close to its N-terminus. The 2.3Å crystal structure of the D3st (stabilized) fragment reveals a mostly parallel α-helical bundle structure in its N-terminal half which smoothly continues into a left-handed CC towards the C-terminus. This provides a direct evidence for a continuously α-helical structure of the coil2 segment and disproves the previously suggested existence of linker L2 separating it into two left-handed CCs. The general principles of CC dimer stabilization by disulfide introduction are also discussed.
ISSN: 1047-8477
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Biocrystallography
× corresponding author
# (joint) last author

Files in This Item:
File Description Status SizeFormat
chernyatina_strelkov_jsb2012[1].pdf Published 1232KbAdobe PDFView/Open Request a copy

These files are only available to some KU Leuven Association staff members


All items in Lirias are protected by copyright, with all rights reserved.

© Web of science