Sandbox Ruth01
From Proteopedia
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Some 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. | Some 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 (light blue) <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 peptide inhibitors, and as a general model for biophysical studies on protein folding. | + | Structurally tendamistat belongs to the scoop class of all beta proteins since it is exclusivly formed of beta sheets (light blue) <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 peptide inhibitors <ref> pmid 15777278</ref>, and as a general model for biophysical studies on protein folding. |
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Revision as of 12:45, 6 September 2012
Your Heading Here (maybe something like 'Structure')
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