Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis.

@article{Chung2004CollagenaseUT,
  title={Collagenase unwinds triple-helical collagen prior to peptide bond hydrolysis.},
  author={Linda C. Chung and Deendayal Dinakarpandian and Naoto Yoshida and Janelle L Lauer-Fields and Gregg B Fields and Robert Visse and Hideaki Nagase},
  journal={The EMBO journal},
  year={2004},
  volume={23 15},
  pages={3020-30}
}
Breakdown of triple-helical interstitial collagens is essential in embryonic development, organ morphogenesis and tissue remodelling and repair. Aberrant collagenolysis may result in diseases such as arthritis, cancer, atherosclerosis, aneurysm and fibrosis. In vertebrates, it is initiated by collagenases belonging to the matrix metalloproteinase (MMP) family. The three-dimensional structure of a prototypic collagenase, MMP-1, indicates that the substrate-binding site of the enzyme is too… CONTINUE READING
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