Sandbox Reserved 1125: Difference between revisions
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Besides the modification of TIMPs, the research for MMPs inhibitors resulted in the discovering of molecules with the ability to interact with the catalytic domain of MMPs. The first developped synthetic inhibitors were molecules that mimic the natural substrates of MMPs combined with a zinc chelating groupement.<ref>PMID:19712708</ref> | Besides the modification of TIMPs, the research for MMPs inhibitors resulted in the discovering of molecules with the ability to interact with the catalytic domain of MMPs. The first developped synthetic inhibitors were molecules that mimic the natural substrates of MMPs combined with a zinc chelating groupement.<ref>PMID:19712708</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/2'>N-hydroxyurea</scene> for MMP-8.<ref>http://www.rcsb.org/pdb/explore/explore.do?structureId=1ZP5</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/2'>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/2'>new inhibitors</scene> of MMP-8.<ref>http://www.rcsb.org/pdb/explore/explore.do?structureId=3DPE</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/2'>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> | ||
== Function == | == Function == | ||
