Journal:JBSD:29
From Proteopedia
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Insulin-degrading enzyme (IDE) is a zinc-metalloendopeptidase found mostly in cytosol. Since overexpression of IDE increases the rate of extracellular insulin degradation, IDE is a potential target for controlling insulin degradation. | Insulin-degrading enzyme (IDE) is a zinc-metalloendopeptidase found mostly in cytosol. Since overexpression of IDE increases the rate of extracellular insulin degradation, IDE is a potential target for controlling insulin degradation. | ||
| - | The binding site of IDE protein bound with insulin (colored in cyan and magenta) is shown by the crystal structure 2G54. Leissring et al. also indicated a series of residues (colored in orange) and zinc ion in the catalytic site of IDE protein which interacted with their IDE inhibitors. | + | The <scene name='Journal:JBSD:29/Cv/3'>binding site of IDE protein bound with insulin</scene> (colored in cyan and magenta) is shown by the crystal structure 2G54. Leissring et al. also indicated a series of residues (colored in orange) and zinc ion in the catalytic site of IDE protein which interacted with their IDE inhibitors. |
Virtual screening of the IDE protein (PDB ID: 2JG4) was conducted using the binding site defined by the catalytic site of IDE protein. In silico results indicate that traditional Chinese medicine compounds dihydrocaffeic acid, isopraeroside IV, and scopolin had high binding affinity with IDE protein and formed hydrogen bonds with the key active residue, Glu111 (colored in magenta) and other residues in the IDE binding site (colored in olive). As the top three TCM compounds had stable interactions with zinc cation and residues in the catalytic site of IDE, they may block binding of other substrates, such as insulin, to the catalytic site. This competitive binding may limit the degradation of insulin. The top TCM candidates, dihydrocaffeic acid, isopraeroside IV, and scopolin, may have potential to be lead compounds for controlling insulin degradation for type 2 diabetes mellitus. | Virtual screening of the IDE protein (PDB ID: 2JG4) was conducted using the binding site defined by the catalytic site of IDE protein. In silico results indicate that traditional Chinese medicine compounds dihydrocaffeic acid, isopraeroside IV, and scopolin had high binding affinity with IDE protein and formed hydrogen bonds with the key active residue, Glu111 (colored in magenta) and other residues in the IDE binding site (colored in olive). As the top three TCM compounds had stable interactions with zinc cation and residues in the catalytic site of IDE, they may block binding of other substrates, such as insulin, to the catalytic site. This competitive binding may limit the degradation of insulin. The top TCM candidates, dihydrocaffeic acid, isopraeroside IV, and scopolin, may have potential to be lead compounds for controlling insulin degradation for type 2 diabetes mellitus. | ||
Revision as of 09:52, 12 September 2012
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- ↑ REF
This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
