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Updated: Oct 4, 2026

Actin Co-Sedimentation Assay; for the Analysis of Protein Binding to F-Actin
Published on: March 28, 2008
Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex
R A Atkinson1, C Joseph, G Kelly
1Division of Molecular Structure, National Institute for Medical Research, The Ridgeway, Mill Hill, London, NW7 1AA UK.
Abstract:
The interaction between alpha-actinin and titin, two modular muscle proteins, is essential for sarcomere assembly. We have solved the solution structure of a complex between the calcium-insensitive C-terminal EF-hand domain of alpha-actinin-2 and the seventh Z-repeat of titin. The structure of the complex is in a semi-open conformation and closely resembles that of myosin light chains in their complexes with heavy chain IQ motifs. However, no IQ motif is present in the Z-repeat, suggesting that the semi-open conformation is a general structural solution for calcium-independent recognition of EF-hand domains.
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