Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors

@article{Lovejoy1999CrystalSO,
  title={Crystal structures of MMP-1 and -13 reveal the structural basis for selectivity of collagenase inhibitors},
  author={Brett Lovejoy and Anthony R. Welch and Steven Carr and Christine Luong and Chris Allen Broka and Robert Than Hendricks and Jeffery A. Campbell and Keith A.M. Walker and Robert Bruce. Martin and Harold E. van Wart and Michelle F. Browner},
  journal={Nature Structural Biology},
  year={1999},
  volume={6},
  pages={217-221}
}
The X-ray crystal structures of the catalytic domain of human collagenase-3 (MMP-13) and collagenase-1 (MMP-1) with bound inhibitors provides a basis for understanding the selectivity profile of a novel series of matrix metalloprotease (MMP) inhibitors. Differences in the relative size and shape of the MMP S1' pockets suggest that this pocket is a critical determinant of MMP inhibitor selectivity. The collagenase-3 S1' pocket is long and open, easily accommodating large P1' groups, such as… CONTINUE READING

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