Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.

@article{Exposito1990CharacterizationOA,
  title={Characterization of a fibrillar collagen gene in sponges reveals the early evolutionary appearance of two collagen gene families.},
  author={J Y Exposito and Robert Garrone},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={1990},
  volume={87 17},
  pages={6669-73}
}
We have characterized cDNA and genomic clones coding for a sponge collagen. The partial cDNA has an open reading frame encoding 547 amino acid residues. The conceptual translation product contains a probably incomplete triple-helical domain (307 amino acids) with one Gly-Xaa-Yaa-Zaa imperfection in the otherwise perfect Gly-Xaa-Yaa repeats and a carboxyl propeptide (240 amino acids) that includes 7 cysteine residues. Amino acid sequence comparisons indicate that this sponge collagen is… CONTINUE READING

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