Title: Simultaneous Formation of Right- and Left-handed Anti-parallel Coiled-coil Interfaces by a Coil2 Fragment of Human Lamin A
Authors: Kapinos, Larisa E
Burkhard, Peter
Herrmann, Harald
Aebi, Ueli
Strelkov, Sergei # ×
Issue Date: Apr-2011
Publisher: Academic Press
Series Title: Journal of Molecular Biology vol:408 issue:1 pages:135-146
Abstract: The elementary building block of all intermediate filaments (IFs) is a dimer featuring a central a-helical rod domain flanked by the N- and C-terminal end domains. In nuclear IF proteins (lamins), the rod domain consists of two coiled-coil segments, coil1 and coil2, that are connected by a short non-helical linker. Coil and the C-terminal part of coil2 contain the two highly conserved IF consensus motifs involved in the longitudinal assembly of dimers. The previously solved crystal structure of a lamin A fragment (residues 305-387) corresponding to the second half of coil2 has yielded a parallel left-handed coiled coil. Here, we present the crystal structure and solution properties of another human lamin A fragment (residues 328-398), which is largely overlapping with fragment 305-387 but harbors a short segment of the tail domain. Unexpectedly, no parallel coiled coil forms within the crystal. Instead, the a-helices are arranged such that two anti-parallel coiled-coil interfaces are formed. The most significant interface has a right-handed geometry, which is accounted for by a characteristic 15-residue repeat pattern that overlays with the canonical heptad repeat pattern. The second interface is a left-handed anti-parallel coiled coil based on the predicted heptad repeat pattern. In solution, the fragment reveals only a weak dimerization propensity. We speculate that the C-terminus of coil2 might unzip, thereby allowing for a right-handed coiled-coil interface to form between two laterally aligned dimers. Such an interface might co-exist with a heterotetrameric left-handed coiled-coil assembly, which is expected to be responsible for the longitudinal A(CN) contact. (C) 2011 Elsevier Ltd. All rights reserved.
ISSN: 0022-2836
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
Kapinos_2011[1].pdf Published 764KbAdobe 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