ArticleThe Journal of biological chemistry2012
The structure of vimentin linker 1 and rod 1B domains characterized by site-directed spin-labeling electron paramagnetic resonance (SDSL-EPR) and X-ray crystallography.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- Unraveling the molecular mechanisms of vimentin interaction with G-quadruplex repeats.Nucleic acids research · 2026Article
- Insights into the Structure of Intermediate Filaments.Sub-cellular biochemistry · 2026Review
- Vimentin Fragmentation and Its Role in Amyloid-Beta Plaque Deposition in Alzheimer's Disease.International journal of molecular sciences · 2025Article
- Deciphering vimentin assembly: Bridging theoretical models and experimental approaches.Molecules and cells · 2024Review
- Filament structure and subcellular organization of the bacterial intermediate filament-like protein crescentin.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Molecular structure of soluble vimentin tetramers.Scientific reports · 2023Article
- Stability profile of vimentin rod domain.Protein science : a publication of the Protein Society · 2022Article
- Impact of N-Terminal Tags on De Novo Vimentin Intermediate Filament Assembly.International journal of molecular sciences · 2022Article
- Biomarker Potential of Vimentin in Oral Cancers.Life (Basel, Switzerland) · 2022Review
- Review
- Structural basis of meiotic chromosome synaptic elongation through hierarchical fibrous assembly of SYCE2-TEX12.Nature structural & molecular biology · 2021Article
- Molecular Insight into the Regulation of Vimentin by Cysteine Modifications and Zinc Binding.Antioxidants (Basel, Switzerland) · 2021Article
- Recent insight into intermediate filament structure.Current opinion in cell biology · 2021Review
- The vimentin cytoskeleton: when polymer physics meets cell biology.Physical biology · 2020Article
- 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
- Binding of the periplakin linker requires vimentin acidic residues D176 and E187.Communications biology · 2020Article
- 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
- Structural basis for lamin assembly at the molecular level.Nature communications · 2019Article
- Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity.Nature communications · 2019Article
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10 authors.
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Abstract
Despite the passage of ∼30 years since the complete primary sequence of the intermediate filament (IF) protein vimentin was reported, the structure remains unknown for both an individual protomer and the assembled filament. In this report, we present data describing the structure of vimentin linker 1 (L1) and rod 1B. Electron paramagnetic resonance spectra collected from samples bearing site-directed spin labels demonstrate that L1 is not a flexible segment between coiled-coils (CCs) but instead forms a rigid, tightly packed structure. An x-ray crystal structure of a construct containing L1 and rod 1B shows that it forms a tetramer comprising two equivalent parallel CC dimers that interact with one another in the form of a symmetrical anti-parallel dimer. Remarkably, the parallel CC dimers are themselves asymmetrical, which enables them to tetramerize rather than undergoing higher order oligomerization. This functionally vital asymmetry in the CC structure, encoded in the primary sequence of rod 1B, provides a striking example of evolutionary exploitation of the structural plasticity of proteins. EPR and crystallographic data consistently suggest that a very short region within L1 represents a minor local distortion in what is likely to be a continuous CC from the end of rod 1A through the entirety of rod 1B. The concordance of this structural model with previously published cross-linking and spectral data supports the conclusion that the crystallographic oligomer represents a native biological structure.
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