Sandbox 31: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 26: | Line 26: | ||
==Inhibitors== | ==Inhibitors== | ||
There are many inhibitors of cysteine proteases like papain including antipain, cystatin, Hg2+, and Leupeptin. Leupeptin is a commonly studied inhibitor of proteases. It inhibits by binding and interacting with the active site which allows it to block the enzyme's desired protein substrate. There are many <scene name='Sandbox_31/1popligand_contacts/1'>Residues</scene> that interact with Leupeptin in the active site. The predominant interaction is from hydrophobic interactions between Leupeptin and <scene name='Sandbox_31/1pophydrointeract/1'>active site residues</scene>. | There are many inhibitors of cysteine proteases like papain including antipain, cystatin, Hg2+, and Leupeptin. Leupeptin is a commonly studied inhibitor of proteases. It inhibits by binding and interacting with the active site which allows it to block the enzyme's desired protein substrate. There are many <scene name='Sandbox_31/1popligand_contacts/1'>Residues</scene> that interact with Leupeptin in the active site. The predominant interaction is from hydrophobic interactions between Leupeptin and <scene name='Sandbox_31/1pophydrointeract/1'>active site residues</scene>. In addition to hydrophobic interactions, there are also some hydrogen bonding interactions to hold Leupeptin in the active site of papain. Leupeptin works well at blocking papain from its enzymatic duties. | ||
<scene name='Sandbox_31/1pophydrointeract/1'>Hydrophobic Interactions</scene> | <scene name='Sandbox_31/1pophydrointeract/1'>Hydrophobic Interactions</scene> | ||
