1ZP5

Crystal structure of the complex between MMP-8 and a N-hydroxyurea inhibitor

Summary for 1ZP5

• Entry DOI: 10.2210/pdb1zp5/pdb
• Descriptor: Neutrophil collagenase, CALCIUM ION, ZINC ION, ... (5 entities in total)
• Functional Keywords: hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasmic granule: P22894
• Total number of polymer chains: 1
• Total formula weight: 18634.05

Authors

Campestre, C.,Agamennone, M.,Tortorella, P.,Preziuso, S.,Biasone, A.,Gavuzzo, E.,Pochetti, G.,Mazza, F.,Tschesche, H.,Gallina, C. (deposition date: 2005-05-16, release date: 2005-12-06, Last modification date: 2023-08-23)

Primary citation

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., 16:20-24, 2006

PubMed Abstract: 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.

PubMed: 16242329
DOI: 10.1016/j.bmcl.2005.09.057

Experimental method

X-RAY DIFFRACTION (1.8 Å)