@article{83836,
  keywords = {Animals, Protein Conformation, Kinetics, Recombinant Proteins, Binding Sites, Recombinant Fusion Proteins, Amino Acid Sequence, Carrier Proteins, Transfection, Fibronectins, Baculoviridae, Spodoptera, Electrophoresis, Polyacrylamide Gel, Models, Structural, Molecular Weight, Maltose, Maltose-Binding Proteins},
  author = {Aguirre and McCormick and Schwarzbauer},
  title = {Fibronectin self-association is mediated by complementary sites within the amino-terminal one-third of the molecule.},
  abstract = {<p>The formation of a fibrillar fibronectin (FN) extracellular matrix requires self-association of FN dimers. In this report, we show that the major sites for self-association are the amino-terminal repeats I1-5 and the first type III repeats. Recombinant FNs and fragments were generated by baculovirus expression of cysteine-rich domains and by bacterial expression of type III repeats as fusion proteins with maltose binding protein. When recombinant polypeptides were immobilized on microtiter wells, FN bound to 70-kDa amino-terminal fragment and to fusion proteins containing repeats III1-2 and III1-6 but not to other type III repeats. Similar results were obtained with a gel overlay assay. Binding was concentration-dependent and saturable. The amino-terminal binding site for III1-2 was further localized to repeats I1-5. Therefore, at least two different sites for FN-FN interaction reside near the amino terminus of the molecule. A model for the regulation of FN matrix assembly is proposed based on intramolecular interactions between these amino-terminal sites.</p>
},
  year = {1994},
  journal = {J Biol Chem},
  volume = {269},
  pages = {27863-8},
  month = {11/1994},
  issn = {0021-9258},
  language = {eng},
}