Sandbox Ruth01
From Proteopedia
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<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=''> | ||
| - | Tendemistat description 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 produced by | + | 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 potentalpha-amylase inhibitor which specifically affects mammalian enzymes, and has no effect on alpha-amylases from other sources (e.g. plant 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>. |
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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." | 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." | ||
Revision as of 12:34, 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
- ↑ 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
