Sandbox 34: Difference between revisions
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<Structure load='9pap' size=' | <Structure load='9pap' size='500' frame='true' align='left' caption='Papain' scene='Sandbox_34/Entire_protein_with_ligandscys/1' /> | ||
== Structure == | == Structure == | ||
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There are many inhibitors for papain because of its broad specificity. It is often used as a model enzyme for those in the papain superfamily, such as cathepsin L and cathepsin K. The inhibition of papain is usually due to active site restriction of cysteine-25 and histidine-159. An interesting inhibitor for cathepsin L developed using papain as the model protease is that of <scene name='Sandbox_34/Clik148_inhibitor/1'>Clik148</scene>. This inhibitor uses both prime and non-prime sites to inhibit papain.<ref> PMID:10600517 </ref> In two different cathepsin K inhibitors, referenced PDB codes <scene name='Sandbox_34/Cathepsin_k_1bp4/1'>1BP4</scene> and <scene name='Sandbox_34/Cathepsin_k_1bqi/1'>1BQI</scene>, it is evident that the inhibitor binds with much closer proximity than that of Clik148. | There are many inhibitors for papain because of its broad specificity. It is often used as a model enzyme for those in the papain superfamily, such as cathepsin L and cathepsin K. The inhibition of papain is usually due to active site restriction of cysteine-25 and histidine-159. An interesting inhibitor for cathepsin L developed using papain as the model protease is that of <scene name='Sandbox_34/Clik148_inhibitor/1'>Clik148</scene>. This inhibitor uses both prime and non-prime sites to inhibit papain.<ref> PMID:10600517 </ref> In two different cathepsin K inhibitors, referenced PDB codes <scene name='Sandbox_34/Cathepsin_k_1bp4/1'>1BP4</scene> and <scene name='Sandbox_34/Cathepsin_k_1bqi/1'>1BQI</scene>, it is evident that the inhibitor binds with much closer proximity than that of Clik148. | ||
