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An atomic model of fimbrin binding to F-actin and its implications for filament crosslinking and regulation

An Erratum to this article was published on 01 October 1998

Abstract

Using a new procedure that combines electron-density correlation with biochemical information, we have fitted the crystal structure of the N-terminal actin-binding domain of human T-fimbrin to helical reconstructions of fimbrin-decorated actin filaments. The map locates the N-terminal calcium-binding domain and identifies actin-binding site residues on the two calponin-homology domains of fimbrin. Based on this map, we propose a model of a fimbrin crosslink in an actin bundle and its regulation by calcium.

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Figure 1: Modular organization of the calponin-homology (CH) domain superfamily.
Figure 2: A representative fit of the fimbrin (ABD1) crystal structure to the 3D reconstruction of the fimbrin–actin complex.
Figure 3: Space filling model of fimbrin (ABD1) with F-actin.
Figure 4: a, (upper panel) Translational scans along the axes of the N375 density.

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Acknowledgements

D.H. and N.V. wish to thank A. Brilliant for his valuable contributions to the graphics displayed in this paper. This work was supported by National Institutes of Health grants to D.DeR., W. L., R. C. (F. S. Fay), S.A. and P.M.

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Hanein, D., Volkmann, N., Goldsmith, S. et al. An atomic model of fimbrin binding to F-actin and its implications for filament crosslinking and regulation. Nat Struct Mol Biol 5, 787–792 (1998). https://doi.org/10.1038/1828

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