Sandbox 39: Difference between revisions

From Proteopedia
Jump to navigationJump to search
Student (talk | contribs)
No edit summary
Student (talk | contribs)
No edit summary
Line 57: Line 57:
Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171.</ref>]]
Hans-Hartwig Otto, and Tanja Schirmeister (1997) Cysteine Proteases and Their Inhibitors. Chemical Reviews. No. 97, 133-171.</ref>]]


<Structure load='9pap' size='300' frame='true' align='right' caption='PAPAIN/ZLFG-DAM COVALENT COMPLEX' scene=''/>
<Structure load='9pap' size='300' frame='true' align='right' caption='Papain/ZLFG-DAM covalent complex' scene=''/>


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.