Mutually exclusive splicing of calcium-binding domain exons in chick alpha-actinin.

@article{Waites1992MutuallyES,
  title={Mutually exclusive splicing of calcium-binding domain exons in chick alpha-actinin.},
  author={G T Waites and Ian R. Graham and Peter Jackson and D B Millake and Bipin D. Patel and Anne Blanchard and Polly A. Weller and I. C. Eperon and David R. Critchley},
  journal={The Journal of biological chemistry},
  year={1992},
  volume={267 9},
  pages={6263-71}
}
We have determined the complete sequence of chick brain alpha-actinin (892 amino acids; 107,644 Da). The sequence differs from that of smooth muscle alpha-actinin only in the region of the first EF-hand calcium-binding motif, where 27 residues in brain alpha-actinin are replaced by just 22 residues in the smooth muscle isoform. This probably accounts for the different calcium sensitivities of the two isoforms with respect to actin binding. Analysis of the gene structure showed that this region… CONTINUE READING

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