1zp5
Crystal structure of the complex between MMP-8 and a N-hydroxyurea inhibitor
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OverviewOverview
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.
About this StructureAbout this Structure
1ZP5 is a Single protein structure of sequence from Homo sapiens with CA, ZN and 2NI as ligands. Active as Neutrophil collagenase, with EC number 3.4.24.34 Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Mon Nov 12 20:38:09 2007