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The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold

Nature Structural Biology volume 4, pages 223–230 (1997)Cite this article

Abstract

The 120,000 Mr gelation factor and α-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are rod-shaped homodimers. Each monomer chain is comprised of an actin-binding domain and a rod domain. The rod domain of the gelation factor consists of six 100-residue repetitive segments with high internal homology. We have now determined the three-dimensional structure of segment 4 of the rod domain of the gelation factor from D. discoideum using NMR spectroscopy. The segment consists of seven β-sheets arranged in an immunoglobulin-like (Ig) fold. This is completely different from the α-actinin rod domain which consists of four spectrin-like α-helical segments. The gelation factor is the first example of an Ig-fold found in an actin-binding protein. Two highly homologous actin-binding proteins from human with similar sequences to the gelation factor, filamin and a 280,000 Mr actin-binding protein (ABP-280), share conserved residues that form the core of the gelation factor repetitive segment structure. Thus, the segment 4 structure should be common to this subfamily of the spectrin super-family. The structure of segment 4 together with previously published electron microscopy data, provide an explanation for the dimerization of the whole gelation factor molecule.

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Authors and Affiliations

  1. Max Planck Institute for Biochemistry, D-82152, Martinsried, F.R.G.

    Paola Fucini, Christian Renner, Christoph Herberhold, Angelika A. Noegel & Tad A. Holak

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  1. Paola Fucini
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Fucini, P., Renner, C., Herberhold, C. et al. The repeating segments of the F-actin cross-linking gelation factor (ABP-120) have an immunoglobulin-like fold. Nat Struct Mol Biol 4, 223–230 (1997). https://doi.org/10.1038/nsb0397-223

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