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>. | + | 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. |
Revision as of 12:42, 6 September 2012
Your Heading Here (maybe something like 'Structure')
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- ↑ Konig V, Vertesy L, Schneider TR. Structure of the alpha-amylase inhibitor tendamistat at 0.93 A. Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1737-43. Epub 2003, Sep 19. PMID:14501112
- ↑ Vertesy L, Oeding V, Bender R, Zepf K, Nesemann G. Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from Streptomyces tendae 4158. Isolation, biochemical properties. Eur J Biochem. 1984 Jun 15;141(3):505-12. PMID:6611258
- ↑ Vertesy L, Oeding V, Bender R, Zepf K, Nesemann G. Tendamistat (HOE 467), a tight-binding alpha-amylase inhibitor from Streptomyces tendae 4158. Isolation, biochemical properties. Eur J Biochem. 1984 Jun 15;141(3):505-12. PMID:6611258
- ↑ Wiegand G, Epp O, Huber R. The crystal structure of porcine pancreatic alpha-amylase in complex with the microbial inhibitor Tendamistat. J Mol Biol. 1995 Mar 17;247(1):99-110. PMID:7897663 doi:http://dx.doi.org/10.1006/jmbi.1994.0125
- ↑ Konig V, Vertesy L, Schneider TR. Structure of the alpha-amylase inhibitor tendamistat at 0.93 A. Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1737-43. Epub 2003, Sep 19. PMID:14501112
