@article{180436,
  keywords = {Animals, Protein Conformation, Base Sequence, Rats, Genes, RNA, Messenger, Binding Sites, Amino Acid Sequence, Macromolecular Substances, Fibronectins, Cell Adhesion, Molecular Weight, Heparin, RNA Splicing},
  author = {Hynes and Schwarzbauer and Tamkun},
  title = {Fibronectin: a versatile gene for a versatile protein},
  abstract = { We have isolated cDNA and genomic clones for rat fibronectins. A single gene gives rise to three different mRNA species by alternative splicing at a complex intron-exon boundary within the coding region. The fibronectins encoded by these three mRNAs differ by the insertion of different protein segments in the C-terminal heparin-binding domain. The amino acid sequences of the cell-, heparin- and fibrin-binding domains in the C-terminal third of fibronectin were deduced from the DNA sequences. The cell- and heparin-binding regions each consist of several similar repeating sequences known as type III homologies, while the fibrin-binding region comprises three repeats of a different type (type I homologies). The sequences suggest several hypotheses for the structure-function relationships of these domains of fibronectin; these hypotheses are now being tested. Determination of intron-exon boundaries within the fibronectin gene is beginning to reveal the modular structure of the gene and its relation to the repeating structure of fibronectin. },
  year = {1984},
  journal = {Ciba Found Symp},
  volume = {108},
  pages = {75-92},
  issn = {0300-5208},
  doi = {10.1002/9780470720899.ch6},
  language = {eng},
}