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The Dictyostelium gelation factor shares a putative actin binding site with alpha-actinins and dystrophin and also has a rod domain containing six 100-residue motifs that appear to have a cross-beta conformation
The 120-kD gelation factor and alpha-actinin are among the most abundant F-actin cross-linking proteins in Dictyostelium discoideum. Both molecules are homodimers and have extended rod-like configurations that are respectively approximately 35 and 40 nm long. Here we report the complete cDNA sequenc...
| Formato: | Texto |
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| Lenguaje: | English |
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The Rockefeller University Press
1989
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| Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2115711/ https://www.ncbi.nlm.nih.gov/pubmed/2668299 |