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1ZS0

Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (S-enantiomer)

Summary for 1ZS0
Entry DOI10.2210/pdb1zs0/pdb
DescriptorNeutrophil collagenase, CALCIUM ION, ZINC ION, ... (6 entities in total)
Functional Keywordsphosphonic inhibitor, sulphonamide junction, stereoselective inhibition, hydrolase
Biological sourceHomo sapiens (human)
Cellular locationCytoplasmic granule: P22894
Total number of polymer chains1
Total formula weight18917.35
Authors
Pochetti, G.,Gavuzzo, E.,Campestre, C.,Agamennone, M.,Tortorella, P.,Consalvi, V.,Gallina, C.,Hiller, O.,Tschesche, H.,Tucker, P.A.,Mazza, F. (deposition date: 2005-05-23, release date: 2006-05-02, Last modification date: 2023-08-23)
Primary citationPochetti, G.,Gavuzzo, E.,Campestre, C.,Agamennone, M.,Tortorella, P.,Consalvi, V.,Gallina, C.,Hiller, O.,Tschesche, H.,Tucker, P.A.,Mazza, F.
Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates.
J.Med.Chem., 49:923-931, 2006
Cited by
PubMed Abstract: Potent and selective inhibitors of matrix metalloproteinases (MMPs), a family of zinc proteases that can degrade all the components of the extracellular matrix, could be useful for treatment of diseases such as cancer and arthritis. The most potent MMP inhibitors are based on hydroxamate as zinc-binding group (ZBG). alpha-Arylsulfonylamino phosphonates incorporate a particularly favorable combination of phosphonate as ZBG and arylsulfonylamino backbone so that their affinity exceptionally attains the nanomolar strength frequently observed for hydroxamate analogues. The detailed mode of binding of [1-(4'-methoxybiphenyl-4-sulfonylamino)-2-methylpropyl]phosphonate has been clarified by the crystal structures of the complexes that the R- and S-enantiomers respectively form with MMP-8. The reasons for the preferential MMP-8 inhibition by the R-phosphonate are underlined and the differences in the mode of binding of analogous alpha-arylsulfonylamino hydroxamates and carboxylates are discussed.
PubMed: 16451058
DOI: 10.1021/jm050787+
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.56 Å)
Structure validation

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