Solution structure of a pair of modules from the gelatin-binding domain of fibronectin

A A Bocquier, J R Potts, A R Pickford, I D Campbell

Research output: Contribution to journalArticlepeer-review


Fibronectin has a role in vital physiological processes such as cell migration during embryogenesis and wound healing. It mediates the attachment of cells to extracellular matrices that contain fibrous collagens. The affinity of fibronectin for native collagen and denatured collagen (gelatin) is located within a 42 kDa domain that contains four type 1 (F1) and two type 2 (F2) modules. A putative ligand-binding site has been located on an isolated F2 module, but the accessibility of this site in the intact domain is unknown. Thus, structural studies of module pairs and larger fragments are required for a better understanding of the interaction between fibronectin and collagen.
Original languageEnglish
Pages (from-to)1451-60
Number of pages10
Issue number12
Publication statusPublished - 1999


  • Amino Acid Sequence
  • Binding Sites
  • Collagen
  • Fibronectins
  • Gelatin
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Nuclear Magnetic Resonance, Biomolecular
  • Protein Structure, Secondary
  • Recombinant Proteins
  • Solutions

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