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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.
Noegel AA, Rapp S, Lottspeich F, Schleicher M, Stewart M. Noegel AA, et al. Among authors: schleicher m. J Cell Biol. 1989 Aug;109(2):607-18. doi: 10.1083/jcb.109.2.607. J Cell Biol. 1989. PMID: 2668299 Free PMC article.
Whereas the sequence of alpha-actinin (Noegel, A., W. Witke, and M. Schleicher. 1987. FEBS [Fed. Eur. Biochem. Soc.] Lett. 221:391-396) suggests that the extended rod domain of the molecule is based on four spectrin-like repeats with high alpha-helix potential, the …
Whereas the sequence of alpha-actinin (Noegel, A., W. Witke, and M. Schleicher. 1987. FEBS [Fed. Eur. Biochem. Soc.] Lett. 221 …
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