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Evidence for the involvement of type II domains in collagen binding by 72 kDa type IV procollagenase
Author(s) -
Bányai László,
Patthy László
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80436-7
Subject(s) - type (biology) , type i collagen , chemistry , collagen, type i, alpha 1 , microbiology and biotechnology , biophysics , biochemistry , biology , extracellular matrix , endocrinology , ecology
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.