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

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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. Access through your institution Buy or


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Download references 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. AUTHOR INFORMATION AUTHORS AND AFFILIATIONS * The W.M. Keck Institute for Cellular Visualization, Brandeis


University, Waltham, 02254, Massachusetts, USA Dorit Hanein & David DeRosier * Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, 02254, Massachusetts, USA


Niels Volkmann * Department of Biochemistry, Albert Einstein College of Medicine, Bronx, 10461, New York, USA Sharon Goldsmith & Steve Almo * Department of Physiology, Boston University


School of Medicine, Boston, 02118, Massachusetts, USA William Lehman * Department of Cell Biology, University of Massachusetts Medical School, Worcester, 01655, Massachusetts, USA Roger


Craig * Department of Biology, Whitehead Institute for Biomedical Research, MIT, Cambridge, 02142, Massachusetts, USA Anne-Marie Michon & Paul Matsudaira Authors * Dorit Hanein View


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permissions ABOUT THIS ARTICLE CITE THIS ARTICLE 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 Download citation * Received: 18 June 1998 * Accepted: 05 August 1998 * Issue Date: September 1998 *


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