Sandbox Ruth01
From Proteopedia
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== Your Heading Here (maybe something like 'Structure') == | == Your Heading Here (maybe something like 'Structure') == | ||
<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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| + | Tendemistat description as found on:[http://supfam.cs.bris.ac.uk/SUPERFAMILY/cgi-bin/scop.cgi?sunid=49498 scoop] | ||
| + | Alpha-amylase inhibitor inhibits mammalian alpha-amylases specifically, by forming a tight stoichiometric 1:1 complex with alpha-amylase. The inhibitor has no action on plant and microbial alpha amylases. | ||
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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>. 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. | ||
Revision as of 10:52, 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
- ↑ 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
