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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: mode of binding in a complex with MMP-8. Campestre, C., Agamennone, M., Tortorella, P., Preziuso, S., Biasone, A., Gavuzzo, E., Pochetti, G., Mazza, F., Hiller, O., Tschesche, H., Consalvi, V., Gallina, C. Bioorg. Med. Chem. Lett. (2006) [Pubmed]
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