Sandbox Reserved 825: Difference between revisions

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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> (L2031, F2039, Y2105, H2106, R2109) suggesting that rapamycin inhibits kinase activity of mTOR by blocking access of the activator phosphatidic acid. 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.

The binding sites for '''phosphatidic acid''' and '''rapamycin''' show significant <scene name='56/568023/Aminoacids_binding_site/3'>overlapping</scene> (L2031, F2039, Y2105, H2106, R2109) suggesting that rapamycin inhibits kinase activity of mTOR by blocking access of the activator phosphatidic acid.

Active residues are exposed to water and interact with the ligand. Passive residues are also in contact with water and are situated proximate to the active ones.<ref> Roterman-Konieczna, Irena. Identification of ligand binding site and protein-protein interaction area. Vol. 8. Springer, 2013. </ref>

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.

<scene name='56/568023/Passive_residues_binding/2'>Three amino acids</scene> 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.

Sandbox Reserved 825: Difference between revisions

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@@ Line 48: / Line 48: @@
 mTOR activity.
-The binding sites for '''phosphatidic acid''' and '''rapamycin''' show significant <scene name='56/568023/Aminoacids_binding_site/3'>overlapping</scene> (L2031, 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 />
+The binding sites for '''phosphatidic acid''' and '''rapamycin''' show significant <scene name='56/568023/Aminoacids_binding_site/3'>overlapping</scene> (L2031, F2039, Y2105, H2106, R2109) suggesting that rapamycin inhibits kinase activity of mTOR by blocking access of the activator phosphatidic acid.<br />
+Active residues are exposed to water and interact with the ligand. Passive residues are also in contact with water and are situated proximate to the active ones.<ref> Roterman-Konieczna, Irena. Identification of ligand binding site and protein-protein interaction area. Vol. 8. Springer, 2013. </ref> <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 />
 <scene name='56/568023/Passive_residues_binding/2'>Three amino acids</scene> 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.