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The Structure of Intermediate Filaments

The Structure of Intermediate Filaments

The intermediate filaments are one of three widely studied cytoskeletal filaments. They are so named as their diameter (10 nm) is in between that of microfilaments (7 nm) and the microtubules (25 nm). These filaments are highly stable and can remain intact when exposed to high salt concentrations and detergents. These filaments are responsible for providing stability and mechanical support to the cells. They also help in cell adhesion and maintaining tissue integrity.
Intermediate filaments...

Formation of Intermediate Filaments

Formation of Intermediate Filaments

Intermediate filaments are cytoskeletal proteins with higher tensile strength and flexibility than microfilaments and microtubules. Unlike the other two cytoskeletal proteins, intermediate filament formation lacks the enzymatic activity to hydrolyze nucleotides like ATP and GTP to generate energy for polymerization. Therefore, the formation of intermediate filaments is multistep self-assembly. The involvement of any accessory proteins in intermediate filament formation has not yet been reported.

Generation of Straight or Branched Actin Filaments

Generation of Straight or Branched Actin Filaments

The straight or branched structure formation of actin filaments is controlled by nucleating proteins such as the formins and Arp2/3 complex. Formin-mediated assembly results in straight filaments, whereas Arp2/3 protein complex-mediated assembly results in branched actin filaments.
Arp2/3 Complex
Arp2/3 complex is a seven-subunit complex consisting of two proteins similar to actin- Arp2 and Arp3, and five other subunits that help keep Arp2 and Arp3 inactive. When required, the complex is...

Formation of Higher-order Actin Filaments

Formation of Higher-order Actin Filaments

The polymerization of G-actin monomers into filamentous F-actin is a multi-step process. Once the F-actins are formed, they can bundle together in different arrangements to form higher-order networks and regulate cellular functions. Common examples include the formation of lamellipodia and filopodia at the cell's leading edge by actin reorganization in a migrating cell. The microvilli on the brush border epithelial cells are also formed through the F-actin network.
The high-order actin networks...

Protein Folding

Protein Folding

Protein Folding

Protein Folding

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Related Experiment Video

Updated: Jun 16, 2026

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Atomic structure of vimentin coil 2.

Stefan Nicolet¹, Harald Herrmann, Ueli Aebi

¹Department of Pharmaceutical Sciences, Katholieke Universiteit Leuven, Belgium.

Journal of Structural Biology

|February 24, 2010

Summary

The crystal structure of a human vimentin fragment reveals a parallel alpha-helical bundle and a coiled coil. This finding aids in building a complete atomic model of the vimentin coil 2 dimer.

Area of Science:

Cell Biology
Structural Biology
Biochemistry

Background:

Intermediate filaments (IFs) are crucial cytoskeletal proteins in animal cells.
IFs assemble from dimers forming a central alpha-helical coiled-coil rod domain.
The rod domain contains coil 1, coil 2, and a linker L12, with coil 2 being conserved in length.

Purpose of the Study:

To determine the crystal structure of a human vimentin fragment corresponding to the first half of coil 2.
To elucidate the structural organization of vimentin coil 2.
To contribute to a complete atomic model of the vimentin coil 2 dimer.

Main Methods:

X-ray crystallography was used to determine the structure of a human vimentin fragment (residues 261-335).
Structural analysis focused on the coiled-coil regions and linker elements within vimentin coil 2.

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Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

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Last Updated: Jun 16, 2026

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Self-assembly of Complex Two-dimensional Shapes from Single-stranded DNA Tiles

Published on: May 8, 2015

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Measuring Interactions of Globular and Filamentous Proteins by Nuclear Magnetic Resonance Spectroscopy (NMR) and Microscale Thermophoresis (MST)

Published on: November 2, 2018

Main Results:

The crystal structure revealed a parallel alpha-helical bundle with 3.5 hendecad repeats followed by a left-handed coiled coil.
The non-helical linker L2 was not observed in this fragment.
Combined with previous data on coil 2B, a complete atomic model of the 21nm vimentin coil 2 dimer was constructed.

Conclusions:

The determined structure provides key insights into the organization of vimentin coil 2.
The vimentin coil 2 dimer is characterized as a relatively rigid rod.
This structural data is essential for understanding intermediate filament assembly and function.