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• W2065943460 abstract "The mode of binding and the activity of the first two non-zinc chelating, potent, and selective inhibitors of human neutrophil collagenase are reported. The crystal structures of the catalytic domain of MMP-8, respectively complexed with each inhibitor, reveals that both ligands are deeply inserted into the primary specificity subsite S1′, where they induce a similar conformational change of the surrounding loop that is endowed with the main specificity determinants of MMPs. Accord to this rearrangement, both inhibitors remove the floor of the pocket formed by the Y227 side-chain, rendering available an extra binding region never explored before. The present data show that potent and more selective inhibitors can be obtained by developing ligands able to interact with the selectivity regions of the enzyme rather than with the catalytic zinc ion, which is the common feature of all MMP members." @default.
• W2065943460 created "2016-06-24" @default.
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• W2065943460 date "2009-01-27" @default.
• W2065943460 modified "2023-09-25" @default.
• W2065943460 title "Extra Binding Region Induced by Non-Zinc Chelating Inhibitors into the S₁′ Subsite of Matrix Metalloproteinase 8 (MMP-8)" @default.
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• W2065943460 doi "https://doi.org/10.1021/jm801166j" @default.
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