Sandbox Reserved 1125: Difference between revisions
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The zinc-binding motif HEXGHXXGXXH presents in the catalytic domain is characteristic for the protease activity of MMP-8. | The zinc-binding motif HEXGHXXGXXH presents in the catalytic domain is characteristic for the protease activity of MMP-8. | ||
===== Zn999 : the catalytic zinc ===== | ===== Zn999 : the catalytic zinc ===== | ||
It is involved in the catalytic activity and is situated at the bottom of the active-site. This ion is penta-coordinated with: His197, His201 and His207 of MMP-8 and with the carbonyl and the hydroxyl oxygen of the hydroxamic acid moiety of the inhibitor. This discovery has been made thanks to the Pro-Leu-Gly-hydroxylamine inhibitor. On this <scene name='71/719866/Zn999_interactions/5'>link</scene> you can only see the 3 His of MMP-8 with the Zn999. The fourth ligand of the catalytic zinc is a water molecule. | It is involved in the catalytic activity and is situated at the bottom of the active-site. This ion is penta-coordinated with: His197, His201 and His207 of MMP-8 and with the carbonyl and the hydroxyl oxygen of the hydroxamic acid moiety of the inhibitor. This discovery has been made thanks to the Pro-Leu-Gly-hydroxylamine inhibitor.<ref name="X-ray"> On this <scene name='71/719866/Zn999_interactions/5'>link</scene> you can only see the 3 His of MMP-8 with the Zn999. The fourth ligand of the catalytic zinc is a water molecule. | ||
[[Image:ZN pocket interaction.gif | thumb|ZN998 pocket interaction]] | [[Image:ZN pocket interaction.gif | thumb|ZN998 pocket interaction]] | ||
===== Zn998 : the structural zinc ===== | ===== Zn998 : the structural zinc ===== | ||