Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.

@article{Stura2013CrystalSO,
  title={Crystal structure of full-length human collagenase 3 (MMP-13) with peptides in the active site defines exosites in the catalytic domain.},
  author={Enrico A Stura and Robert Visse and Philippe Cuniasse and Vincent Dive and Hideaki Nagase},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2013},
  volume={27 11},
  pages={4395-405}
}
Matrix metalloproteinase (MMP)-13 is one of the mammalian collagenases that play key roles in tissue remodelling and repair and in progression of diseases such as cancer, arthritis, atherosclerosis, and aneurysm. For collagenase to cleave triple helical collagens, the triple helical structure has to be locally unwound before hydrolysis, but this process is not well understood. We report crystal structures of catalytically inactive full-length human MMP-13(E223A) in complex with peptides of 14… CONTINUE READING
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