N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: mode of binding in a complex with MMP-8.

@article{Campestre2006NHydroxyureaAZ,
  title={N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: mode of binding in a complex with MMP-8.},
  author={Cristina Campestre and Mariangela Agamennone and Paolo Tortorella and Serena Preziuso and Alessandro Biasone and Enrico Gavuzzo and Giorgio Pochetti and Fernando Mazza and Oliver Hiller and Harald Tschesche and Valerio Consalvi and Carlo Gallina},
  journal={Bioorganic & medicinal chemistry letters},
  year={2006},
  volume={16 1},
  pages={20-4}
}
The first crystallographic structure of an N-hydroxyurea inhibitor bound into the active site of a matrix metalloproteinase is reported. The ligand and three other analogues were prepared and studied as inhibitors of MMP-2, MMP-3, and MMP-8. The crystal structure of the complex with MMP-8 shows that the N-hydroxyurea, contrary to the analogous hydroxamate, binds the catalytic zinc ion in a monodentate rather than bidentate mode and with high out-of-plane distortion of the amide bonds.