1zp5
Crystal structure of the complex between MMP-8 and a N-hydroxyurea inhibitor
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| , resolution 1.80Å | |||||||
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| Ligands: | , and | ||||||
| Gene: | MMP8, CLG1 (Homo sapiens) | ||||||
| Activity: | Neutrophil collagenase, with EC number 3.4.24.34 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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