Sandbox 39: Difference between revisions
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Another example of a papain inhibitor is <scene name='Sandbox_39/Inhibitor/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/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. | ||
== References == | |||
1. Image from: http://upload.wikimedia.org/wikipedia/commons/5/5c/Cysteinprotease_Reaktionsmechanismus.svg | |||
2. Image from: http://en.wikipedia.org/wiki/Papain | |||
3. Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171. | |||
4. Image from: http://www.rcsb.org/pdb/explore/jmol.do?structureId=9PAP&bionumber=1 | |||
5. Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171. | |||
