Sandbox Ruth01

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A crystal structure has been determined for tendamistat the 74-amino acid inhibitor produced by ''Streptomyces tendae'' that targets a wide range of mammalian alpha-amylases <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. The crystal structure of tendamistat revealed an immunoglobulin-like fold that could potentially adopt multiple conformations. Such molecular flexibility could enable an induced-fit type of binding that would both optimise binding and allow broad target specificity."
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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.
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A crystal structure of tendemistat (green) with a pig pancreatic alpha-amylase (orange) is also available <ref> pmid 7897663</ref> <scene name='Sandbox_Ruth01/Complex/1'>complex structure</scene>.
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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>.
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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>.
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Revision as of 12:37, 6 September 2012

Your Heading Here (maybe something like 'Structure')

Structure of Tendamistat reductase (PDB entry 1ok0)

Drag the structure with the mouse to rotate
  1. ↑ 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
  2. ↑ 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
  3. ↑ 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
  4. ↑ 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
  5. ↑ 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
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