Local conformation and dynamics of isoleucine in the collagenase cleavage site provide a recognition signal for matrix metalloproteinases.

@article{Xiao2010LocalCA,
  title={Local conformation and dynamics of isoleucine in the collagenase cleavage site provide a recognition signal for matrix metalloproteinases.},
  author={Jianxi Xiao and Rayna M Addabbo and Janelle L. Lauer and Gregg B Fields and J. M. Baum},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 44},
  pages={34181-90}
}
The mechanism by which enzymes recognize the "uniform" collagen triple helix is not well understood. Matrix metalloproteinases (MMPs) cleave collagen after the Gly residue of the triplet sequence Gly∼[Ile/Leu]-[Ala/Leu] at a single, unique, position along the peptide chain. Sequence analysis of types I-III collagen has revealed a 5-triplet sequence pattern in which the natural cleavage triplets are always flanked by a specific distribution of imino acids. NMR and MMP kinetic studies of a series… CONTINUE READING