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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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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DOI: https://doi.org/10.1038/1828
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