Evidence for the involvement of type II domains in collagen binding by 72 kDa type IV procollagenase.
The fibronectin-related region of the 72 kDa type IV procollagenase has been expressed in E. coli as a beta-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.
Bányai
L
L
Institute of Enzymology, Hungarian Academy of Sciences, Budapest.
Patthy
L
L
D000595:Amino Acid Sequence; D001483:Base Sequence; D001665:Binding Sites; D002846:Chromatography, Affinity; D003001:Cloning, Molecular; D003062:Codon; D003094:Collagen / Q000378:metabolism*; D017364:Collagenases; D004247:DNA; D004792:Enzyme Precursors / Q000235:genetics* / Q000378:metabolism; D004926:Escherichia coli / Q000235:genetics; D005353:Fibronectins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D003012:Microbial Collagenase / Q000235:genetics* / Q000378:metabolism; D008969:Molecular Sequence Data; D015183:Restriction Mapping
D003062:Codon; D004792:Enzyme Precursors; D005353:Fibronectins; D003094:Collagen; D004247:DNA; D017364:Collagenases; C022440:procollagenase; D003012:Microbial Collagenase