Sandbox Reserved 1125: Difference between revisions

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Numerous range of compounds such as hydroxamate, thiol, pyrimidine and phosphorus based-molecules were developped. Those inhibitors inhibit the activity of MMPs by chelating the catalytic zinc like <scene name='71/719866/N-hydroxyurea/4'>N-hydroxyurea</scene> for MMP-8.<ref>[http://www.rcsb.org/pdb/explore/explore.do?structureId=1ZP5 'Crystal structure of the complex between MMP-8 and a N-hydroxyurea inhibitor']</ref>
Numerous range of compounds such as hydroxamate, thiol, pyrimidine and phosphorus based-molecules were developped. Those inhibitors inhibit the activity of MMPs by chelating the catalytic zinc like <scene name='71/719866/N-hydroxyurea/4'>N-hydroxyurea</scene> for MMP-8.<ref>[http://www.rcsb.org/pdb/explore/explore.do?structureId=1ZP5 'Crystal structure of the complex between MMP-8 and a N-hydroxyurea inhibitor']</ref>


Recently, new range of inhibitors which do not chelate the catalytic zinc were developped. Those compounds target the selectivity regions for substrates of the MMPs rather than binding to the catalytic zinc. For instance, they can interact with the S1' pocket and induce a conformational change like <scene name='71/719866/Non-chelating_inhibitor/3'>new inhibitors</scene> of MMP-8.<ref>[http://www.rcsb.org/pdb/explore/explore.do?structureId=3DPE 'Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor']</ref>
Recently, new range of inhibitors which do not chelate the catalytic zinc were developped. Those compounds target the selectivity regions for substrates of the MMPs rather than binding to the catalytic zinc. For instance, they can interact with the S1' pocket and induce a conformational change like <scene name='71/719866/Non-chelating_inhibitor/4'>new inhibitors</scene> of MMP-8.<ref>[http://www.rcsb.org/pdb/explore/explore.do?structureId=3DPE 'Crystal structure of the complex between MMP-8 and a non-zinc chelating inhibitor']</ref>