Evidence for the involvement of type II domains in collagen binding by 72 kDa type IV procollagenase

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The fibronectin-related region of the 72 kDa type IV procollagenase has been expressed in E. coli as a β-galactosidase fusion product. The fragment containing the three type II units of the protein was found to have affinity for denatured collagen, suggesting that these domains may be responsible for the collagen-affinity of type IV collagenase. We have also shown that segment Ala-Ala-His-Glu of type IV collagenase (residues 372-375), which is similar to a fibronectin-segment previously implicated in collagen-binding, is not essential for binding activity.

Original languageEnglish
Pages (from-to)23-25
Number of pages3
JournalFEBS letters
Issue number1
Publication statusPublished - Apr 22 1991



  • Fibronectin
  • Matrix degradation
  • Tissue remodelling
  • Tumor invasion
  • Type IV collagenase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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