Collagenase (matrix metalloproteinase 1) cleaves type I, II, and III collagen helices at a specific site between Gly-Ile or Gly-Leu bonds (residues 775 and 776, Pj-P1'). To understand the mechanism of collagen processing, mutations around the cleavage site have been introduced into the cloned murine proal(I) collagen (Collal) The collagenases cleave native type I, II, and III collagens by hydrolyzing the peptide bond between residues Gly-Ile (or Leu) located at residues 775 and 776 of the helical portion of the al(I) chain to yield a larger three-quarter length fragment (TCA) and a smaller one-quarter length fragment (TCB) (1,4,17). The region around the cleavage site is more hydrophobic than other parts of the collagen molecule and deficient in the hydroxyproline and proline residues that stabilize the triple helix. Our
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