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The structure of an actin-crosslinking domain from human fimbrin

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The structure of the N-terminal actin binding domain of human f imbrin offers the first view of an F-actin crosslinking protein and is representative of the conserved actin binding domain found in the largest family of crosslinking proteins. This domain is composed of two calponin homology domains and allows for the mapping of residues implicated in F-actin binding.

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Author information

Author notes

  1. Navin Pokala

    Present address: Department of Molecular and Cell Biology, University of California, Berkeley, California, 94720, USA

  2. Wenyan Shen

    Present address: Amgen Institute, Toronto, Ontario, Canada

Authors and Affiliations

  1. Dept. of Biochemistry, Albert Einstein College of Medicine, Bronx, New York, 10461, USA

    Sharon C. Goldsmith, Alexander A. Fedorov & Steven C. Almo

  2. Whitehead Institute for Biomedical Research, Massachusetts Institute of Technology, Nine Cambridge Centre, Cambridge, Massachusetts, 02142, USA

    Navin Pokala, Wenyan Shen & Paul Matsudaira

  3. Department of Biology, Massachusetts Institute of Technology, Nine Cambridge Centre, Cambridge, Massachusetts, 02142, USA

    Paul Matsudaira

Authors
  1. Sharon C. Goldsmith
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  2. Navin Pokala
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  3. Wenyan Shen
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  4. Alexander A. Fedorov
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  5. Paul Matsudaira
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  6. Steven C. Almo
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Goldsmith, S., Pokala, N., Shen, W. et al. The structure of an actin-crosslinking domain from human fimbrin. Nat Struct Mol Biol 4, 708–712 (1997). https://doi.org/10.1038/nsb0997-708

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  • DOI: https://doi.org/10.1038/nsb0997-708

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