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Sandbox Ruth01
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| - | == | + | == Tendamistat == |
<StructureSection load='1ok0' size='350' side='right' caption='Structure of Tendamistat reductase (PDB entry [[1ok0]])' scene=''> | <StructureSection load='1ok0' size='350' side='right' caption='Structure of Tendamistat reductase (PDB entry [[1ok0]])' scene=''> | ||
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A few crystal structures have been determined for tendamistat, the latest being determined to a 0.93 A resolution <ref> pmid 14501112</ref> <scene name='Sandbox_Ruth01/Tandemistat_no_changes/1'>Tendamistat</scene>. The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. | A few crystal structures have been determined for tendamistat, the latest being determined to a 0.93 A resolution <ref> pmid 14501112</ref> <scene name='Sandbox_Ruth01/Tandemistat_no_changes/1'>Tendamistat</scene>. The binding of tendamistat to alpha-amylase leads to the steric blockage of the active site of the enzyme. | ||
| - | Structurally tendamistat belongs to the scoop class of all beta proteins since it is exclusivly formed of beta sheets | + | Structurally tendamistat belongs to the scoop class of all beta proteins, since it is exclusivly formed of beta sheets <scene name='Sandbox_Ruth01/Beta_sheet_only/1'>Beta-sheets only</scene>. Former research have concidered tendamistat as a therapoic agent for diabetes mellitus due to its ability to block alpha amylase activity. However, tendamistat was found to be immunogenic, and therefore could not be used as a cure on its own. Currently tendamistat is mainly interesting as a scaffold for designed new peptide inhibitors of alpha-amylase <ref> pmid 15777278</ref>, and as a general model for biophysical studies on protein folding <ref> pmid 11237606</ref>. |
Current revision
Tendamistat
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