ArticleThe FEBS journal2018
A crystal structure of coil 1B of vimentin in the filamentous form provides a model of a high-order assembly of a vimentin filament.
Article in The FEBS journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 23 citations in OpenAlex.
- Insights into the Structure of Intermediate Filaments.Sub-cellular biochemistry · 2026Review
- Designability of α-Helical Protein Filaments.Sub-cellular biochemistry · 2026Review
- Vimentin Dynamics in Viral Infection: Shield or Sabotage?International journal of molecular sciences · 2025Review
- Deciphering vimentin assembly: Bridging theoretical models and experimental approaches.Molecules and cells · 2024Review
- Type III intermediate filaments in redox interplay: key role of the conserved cysteine residue.Biochemical Society transactions · 2024Review
- Add and Go: FRET Acceptor for Live-Cell Measurements Modulated by Externally Provided Ligand.International journal of molecular sciences · 2022Article
- Molecular Docking of SP40 Peptide towards Cellular Receptors for Enterovirus 71 (EV-A71).Molecules (Basel, Switzerland) · 2021Article
- Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12.Nature structural & molecular biology · 2021Article
- Recent insight into intermediate filament structure.Current opinion in cell biology · 2021Review
- Molecular Modeling of Pathogenic Mutations in the Keratin 1B Domain.International journal of molecular sciences · 2020Article
- Structure-Function Analyses of a Keratin Heterotypic Complex Identify Specific Keratin Regions Involved in Intermediate Filament Assembly.Structure (London, England : 1993) · 2020Article
- Redox Regulation of PPARPPAR research · 2020Article
- Article
- Completion of the Vimentin Rod Domain Structure Using Experimental Restraints: A New Tool for Exploring Intermediate Filament Assembly and Mutations.Structure (London, England : 1993) · 2019Article
- Human keratin 1/10-1B tetramer structures reveal a knob-pocket mechanism in intermediate filament assembly.The EMBO journal · 2019Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Vimentin is an intermediate filament (IF) protein that is expressed in leukocytes, fibroblasts and endothelial cells of blood vessels. Vimentin filaments contribute to structural stability of the cell membrane, organelle positioning and protein transport. Vimentin self-assembles into a dimer that subsequently forms high-order structures, including tetramers and octamers. The details of IF assembly at crystallographic resolutions are limited to the tetrameric form. We describe a crystal structure of a fragment of a vimentin rod domain (coil 1B) with a dimer of tetramers in the asymmetric unit. Coil 1B in the crystal is in an infinitely high-order filamentous assembly state, in which the tetramers are packed against each other laterally in an antiparallel fashion across the crystal lattice. In one of the directions of lateral packing, the tetramers pack against each other strictly head-to-tail, and in the orthogonal direction the tetramers pack in a staggered manner. This organization of the tetramers of coil 1B in the crystal lattice, together with previously reported biochemical and structural data, yield a model of high-order vimentin filament assembly. DATABASE: Structural data are available in the PDB under the accession number 5WHF.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.