Sandbox Ruth01
From Proteopedia
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The following Tendemistat description is based on [http://supfam.cs.bris.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=49498 scoop], koning et al. (2003)<ref> pmid 14501112</ref> and Vertesy et al. (1984)<ref> pmid 6611258</ref> : | The following Tendemistat description is based on [http://supfam.cs.bris.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=49498 scoop], koning et al. (2003)<ref> pmid 14501112</ref> and Vertesy et al. (1984)<ref> pmid 6611258</ref> : | ||
| - | Tendemistat is a 74 amino acid protein produced by ''Streptomyces tendae''. Though it has been suggested to perform a regulatory role in its natural producer<ref> pmid 6611258</ref>, its native purpose remains unclear. However, tendamistat was found to be a potent inhibitor of alpha-amylase. Tendamistat was specifically found to affect mammalian enzymes, and has shown no effect on alpha-amylases from other sources | + | Tendemistat is a 74 amino acid protein produced by ''Streptomyces tendae''. Though it has been suggested to perform a regulatory role in its natural producer<ref> pmid 6611258</ref>, its native purpose remains unclear. However, tendamistat was found to be a potent inhibitor of alpha-amylase. Tendamistat was specifically found to affect mammalian enzymes, and has shown no effect on alpha-amylases from other sources such as plants and bacteria. Tendamistat (green) forms a tight stoichiometric 1:1 complex with alpha-amylase (orange), a crystal structure of the complex was determined to a 2.5 A resolution <ref> pmid 7897663</ref> <scene name='Sandbox_Ruth01/Complex/1'>complex structure</scene>. |
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 (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. | 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. | ||
Revision as of 12:51, 6 September 2012
Your Heading Here (maybe something like 'Structure')
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