Journal:JBSD:29
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The <scene name='Journal:JBSD:29/Cv/3'>binding site of IDE protein bound with insulin</scene> (<span style="color:cyan;background-color:black;font-weight:bold;">IDE protein colored in cyan</span> and <font color='darkmagenta'><b>insulin colored in darkmagenta</b></font>) is shown by the crystal structure [[2g54]]. Leissring ''et al.'' (2010)<ref name="Leissring">PMID:20498699</ref> also indicated a <scene name='Journal:JBSD:29/Cv/4'>series of residues</scene> (<span style="color:orange;background-color:black;font-weight:bold;">colored in orange</span>) 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> (<span style="color:cyan;background-color:black;font-weight:bold;">IDE protein colored in cyan</span> and <font color='darkmagenta'><b>insulin colored in darkmagenta</b></font>) is shown by the crystal structure [[2g54]]. Leissring ''et al.'' (2010)<ref name="Leissring">PMID:20498699</ref> also indicated a <scene name='Journal:JBSD:29/Cv/4'>series of residues</scene> (<span style="color:orange;background-color:black;font-weight:bold;">colored in orange</span>) 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 <scene name='Journal:JBSD:29/Cv/5'>dihydrocaffeic acid</scene> (<span style="color:royalblue;background-color:black;font-weight:bold;">colored in royalblue</span>), <scene name='Journal:JBSD:29/Cv/6'>isopraeroside IV</scene> (<font color='blueviolet'><b>colored in blueviolet</b></font>), and scopolin had high binding affinity with IDE protein and formed hydrogen bonds with the key active residue, <font color='magenta'><b>Glu111 (colored in magenta)</b></font> and <span style="color:lime;background-color:black;font-weight:bold;">other residues in the IDE binding site (colored in green)</span>. 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 <scene name='Journal:JBSD:29/Cv/5'>dihydrocaffeic acid</scene> (<span style="color:royalblue;background-color:black;font-weight:bold;">colored in royalblue</span>), <scene name='Journal:JBSD:29/Cv/6'>isopraeroside IV</scene> (<font color='blueviolet'><b>colored in blueviolet</b></font>), and <scene name='Journal:JBSD:29/Cv/8'>scopolin</scene> (<span style="color:chocolate;background-color:black;font-weight:bold;">colored in chocolate</span>) had high binding affinity with IDE protein and formed hydrogen bonds with the key active residue, <font color='magenta'><b>Glu111 (colored in magenta)</b></font> and <span style="color:lime;background-color:black;font-weight:bold;">other residues in the IDE binding site (colored in green)</span>. 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. |
</StructureSection> | </StructureSection> | ||
<references/> | <references/> | ||
__NOEDITSECTION__ | __NOEDITSECTION__ | ||
Revision as of 12:12, 12 September 2012
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- ↑ REF
- ↑ Leissring MA, Malito E, Hedouin S, Reinstatler L, Sahara T, Abdul-Hay SO, Choudhry S, Maharvi GM, Fauq AH, Huzarska M, May PS, Choi S, Logan TP, Turk BE, Cantley LC, Manolopoulou M, Tang WJ, Stein RL, Cuny GD, Selkoe DJ. Designed inhibitors of insulin-degrading enzyme regulate the catabolism and activity of insulin. PLoS One. 2010 May 7;5(5):e10504. PMID:20498699 doi:10.1371/journal.pone.0010504
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.
