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Chuck Reynolds
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What does Resveratrol induce.? P-8

Published on 6/16/2019
For additional information  Click Here

Resveratrol induces autophagy by directly inhibiting mTOR through ATP competition P-8

Computational simulation of the interaction between mTOR and resveratrol

To assess the mode of action for inhibiting the kinase activity of mTOR, we carried out docking simulations of resveratrol in the ATP-binding site of mTOR for determining the lowest-energy binding mode of resveratrol.   Resveratrol appears to be stabilized in the binding pocket formed by the Gly loop, hinge region of the ATP-binding site, and the interface residues of N- and C-terminal domains.

To examine the possibility of allosteric inhibition of mTOR by resveratrol, we performed additional docking simulations with extended 3D grid maps that include the whole kinase domain. However, no peripheral binding site was found in which resveratrol could be stabilized with negative free energy of binding. It is thus expected that the micromolar-level inhibitory activity of resveratrol against mTOR stems from the specific binding in the ATP binding site.

We now address the detailed interactions responsible for stabilization of resveratrol in the ATP-binding pocket. The binding mode of resveratrol calculated from docking simulations is shown in. We observed that the terminal phenolic group of resveratrol receives and donates a hydrogen bond from the backbone amidic nitrogen to the aminocarbonyl oxygen of V2240, respectively.

This hydrogen bond seems to be important for the biochemical potency of resveratrol because the formation of hydrogen bonds with same region was also observed in the structures of mTOR complex with potent inhibitors. In the assessed mTOR-resveratrol complex, two additional hydrogen bonds are established between the benzene-1,3-diol moiety and the side-chain carboxylate groups of E2190 and D2195. On the basis from docking simulations, it can be argued that the inhibitory activity of resveratrol can be attributed to the multiple hydrogen bonds.

Article Produced By
Department of Life Sciences, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea
School of Interdisciplinary Bioscience and Bioengineering, Pohang University of Science and Technology, Pohang 790-784, Republic of Korea
School of Life Sciences, Ulsan National Institute of Science and Technology, Ulsan 689-798, Republic of Korea
Department of Bioscience and Biotechnology, Sejong University, 98 Kunja-Dong, Kwangjin-Ku, Seoul 143-747, Republic of Korea

(All these Articles can be read with this URL: )

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Chuck Reynolds

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