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Updated: Jun 13, 2026

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
Published on: March 28, 2008
The domain structure of talin: residues 1815-1973 form a five-helix bundle containing a cryptic vinculin-binding site
Benjamin T Goult1, Alexandre R Gingras, Neil Bate
1Department of Biochemistry, University of Leicester, Leicester, UK.
Abstract:
Talin is a large flexible rod-shaped protein that activates the integrin family of cell adhesion molecules and couples them to cytoskeletal actin. Its rod region consists of a series of helical bundles. Here we show that residues 1815-1973 form a 5-helix bundle, with a topology unique to talin which is optimally suited for formation of a long rod such as talin. This is much more stable than the 4-helix (1843-1973) domain described earlier and as a result its vinculin binding sequence is inaccessible to vinculin at room temperature, with implications for the overall mechanism of the talin-vinculin interaction.
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