Sandbox Reserved 825: Difference between revisions
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The surface structure reveals two main interaction sites, a shallow <scene name='56/568023/Hydrophobic_pocket/1'>hydrophobic patch</scene> made up by helix 1 and helix 4 | The surface structure reveals two main interaction sites, a shallow <scene name='56/568023/Hydrophobic_pocket/1'>hydrophobic patch</scene> made up by helix 1 and helix 4 | ||
which is responsible for the binding of rapamycin | which is responsible for the binding of rapamycin and a <scene name='56/568023/Deep_cleft_helix_2_and_3/1'>deep cleft</scene> between helix 2 and helix 3. This cleft contains | ||
charged and hydrophobic residues and is expected to function as a binding site for small molecules to regulate | charged and hydrophobic residues and is expected to function as a binding site for small molecules to regulate | ||
mTOR activity. | mTOR activity. | ||
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are also capable of inhibiting the kinase activity of mTOR by partially occupying the binding site for phosphatidic acid. | are also capable of inhibiting the kinase activity of mTOR by partially occupying the binding site for phosphatidic acid. | ||
There are <scene name='56/568023/Hts-1_binding_residues/1'>ten</scene> residues at the FRB domain that are predominantly involved in HTS-1 binding. At least <scene name='56/568023/Ovelap_pa_and_hts-1/1'>six</scene> of those residues also take part in phosphatidic acid | There are <scene name='56/568023/Hts-1_binding_residues/1'>ten</scene> residues at the FRB domain that are predominantly involved in HTS-1 binding. At least <scene name='56/568023/Ovelap_pa_and_hts-1/1'>six</scene> of those residues also take part in phosphatidic acid | ||
binding. <ref> PMID:17684489 </ref> | binding. <ref> PMID: 17684489 </ref> | ||
{{clear}} | {{clear}} | ||
