Sandbox Reserved 825: Difference between revisions

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OCA, Dimitri Feltrin, Hamelin Baptiste

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 mTOR activity.
-The binding sites for '''phosphatidic acid''' and '''rapamycin''' show significant <scene name='56/568023/Aminoacids_binding_site/3'>overlapping</scene> (E2031, F2039, Y2105, H2106, R2109) suggesting that rapamycin inhibits kinase activity of mTOR by blocking access of the activator phosphatidic acid.<br /> There are five amino acids whose side chains are exposed to the solvent and who play an active role in phosphatidic acid binding (E2031, F2039, Y2105, H2106, R2109). Those are the residues that also take part in rapamycin binding. Three amino acids at the FRB domain contribute passively to the binding of the activator (L2031, S2035, W2101). The positive charged arginine residue '''R2109''' plays a key role in the binding of phosphatidic acid as it binds to the negetively charged phosphate group.
+The binding sites for '''phosphatidic acid''' and '''rapamycin''' show significant <scene name='56/568023/Aminoacids_binding_site/3'>overlapping</scene> (E2031, F2039, Y2105, H2106, R2109) suggesting that rapamycin inhibits kinase activity of mTOR by blocking access of the activator phosphatidic acid.<br /> There are <scene name='56/568023/Aminoacids_binding_site2/1'>five amino acids </scene>whose side chains are exposed to the solvent and who play an active role in phosphatidic acid binding (E2031, F2039, Y2105, H2106, R2109). Those are the residues that also take part in rapamycin binding.<br />
+Three amino acids at the FRB domain contribute passively to the binding of the activator (L2031, S2035, W2101). The positive charged arginine residue '''R2109''' plays a key role in the binding of phosphatidic acid as it binds to the negetively charged phosphate group.
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