Sandbox 39: Difference between revisions
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Another example of a papain inhibitor is <scene name='Sandbox_39/Inhibitor_revised/1'>ZLFG-DAM</scene>, a diazomethylketone inhibitor. As shown in the Jmol to the right, the methylene carbon atom of the inhibitor (shown as a grey sphere), is covalently bound to the Cys-25 of papain. The hydrophobic S2 pocket is occupied by the inhibitor's P2 side chain, shown as a pink chain. Extensive hydrogen bonding and hydrophobic interactions are responsible for the interaction of the inhibitor with the enzyme. | Another example of a papain inhibitor is <scene name='Sandbox_39/Inhibitor_revised/1'>ZLFG-DAM</scene>, a diazomethylketone inhibitor. As shown in the Jmol to the right, the methylene carbon atom of the inhibitor (shown as a grey sphere), is covalently bound to the Cys-25 of papain. The hydrophobic S2 pocket is occupied by the inhibitor's P2 side chain, shown as a pink chain. Extensive hydrogen bonding and hydrophobic interactions are responsible for the interaction of the inhibitor with the enzyme. | ||
Several other molecules have been shown to have protease inhibitory actions. Leupeptin is a naturally-occuring, microbial protease inhibitor. Shown to the left, sitting in the active site of papain, this molecule contains an arginine residue at its C-terminus that is essential for its inhibitory action. | |||
[[Image:Leupeptin.jpg|left]] | |||
<ref>Image from: | |||
http://www.rcsb.org/pdb/explore/explore.do?structureId=1POP</ref>]] | |||
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