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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 787-792 |
| Number of pages | 6 |
| Journal | Nature structural biology |
| Volume | 5 |
| Issue number | 9 |
| DOIs | |
| State | Published - Sep 9 1998 |
| Externally published | Yes |
ASJC Scopus subject areas
- Structural Biology
- Biochemistry
- Genetics
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Cite this
Hanein, D., Volkmann, N., Goldsmith, S., Michon, A. M., Lehman, W., Craig, R., DeRosier, D., Almo, S., & Matsudaira, P. (1998). An atomic model of fimbrin binding to F-actin and its implications for filament crosslinking and regulation. Nature structural biology, 5(9), 787-792. https://doi.org/10.1038/1828