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==Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (S-enantiomer)== | ==Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (S-enantiomer)== | ||
<StructureSection load='1zs0' size='340' side='right' caption='[[1zs0]], [[Resolution|resolution]] 1.56Å' scene=''> | <StructureSection load='1zs0' size='340' side='right' caption='[[1zs0]], [[Resolution|resolution]] 1.56Å' scene=''> | ||
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP8, CLG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MMP8, CLG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Neutrophil_collagenase Neutrophil collagenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.34 3.4.24.34] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zs0 OCA], [http://pdbe.org/1zs0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zs0 RCSB], [http://www.ebi.ac.uk/pdbsum/1zs0 PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zs0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zs0 OCA], [http://pdbe.org/1zs0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1zs0 RCSB], [http://www.ebi.ac.uk/pdbsum/1zs0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1zs0 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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</div> | </div> | ||
<div class="pdbe-citations 1zs0" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1zs0" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 14:09, 12 October 2017
Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (S-enantiomer)Crystal structure of the complex between MMP-8 and a phosphonate inhibitor (S-enantiomer)
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 PubMedPotent 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. Structural insight into the stereoselective inhibition of MMP-8 by enantiomeric sulfonamide phosphonates.,Pochetti G, Gavuzzo E, Campestre C, Agamennone M, Tortorella P, Consalvi V, Gallina C, Hiller O, Tschesche H, Tucker PA, Mazza F J Med Chem. 2006 Feb 9;49(3):923-31. PMID:16451058[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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