Structural highlights
Function
[MMP8_HUMAN] Can degrade fibrillar type I, II, and III collagens.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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 Jan 1;16(1):20-4. Epub 2005 Oct 18. PMID:16242329[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Campestre C, Agamennone M, Tortorella P, Preziuso S, Biasone A, Gavuzzo E, Pochetti G, Mazza F, Hiller O, Tschesche H, Consalvi V, Gallina C. N-Hydroxyurea as zinc binding group in matrix metalloproteinase inhibition: mode of binding in a complex with MMP-8. Bioorg Med Chem Lett. 2006 Jan 1;16(1):20-4. Epub 2005 Oct 18. PMID:16242329 doi:10.1016/j.bmcl.2005.09.057
