Sandbox 34: Difference between revisions

Line 47:

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.

Sandbox 34: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

Revision as of 08:27, 14 November 2011 view source Student (talk \| contribs) students 33,923 edits No edit summary ← Older edit		Revision as of 08:29, 14 November 2011 view source Student (talk \| contribs) students 33,923 edits No edit summary Newer edit →
Line 47:		Line 47:

	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.