Sandbox Reserved 825: Difference between revisions
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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/2'>ten</scene> residues at the FRB domain that are predominantly involved in HTS-1 binding | There are <scene name='56/568023/Hts-1_binding_residues/2'>ten</scene> residues at the FRB domain that are predominantly involved in HTS-1 binding | ||
( | (active residues: E2032, S2035, Y2038, F2039, T2098, W2101, Y2105, F2108, passive residues: H2028, L2031). <br /> | ||
At least <scene name='56/568023/Ovelap_pa_and_hts-1/4'>six</scene> of those residues also take part in phosphatidic acid binding (L2031, W2101, E2032, F2039, Y2105, S2035). <ref> DOI: 10.1007/s12154-008-0003-5 | At least <scene name='56/568023/Ovelap_pa_and_hts-1/4'>six</scene> of those residues also take part in phosphatidic acid binding (L2031, W2101, E2032, F2039, Y2105, S2035). <ref> DOI: 10.1007/s12154-008-0003-5 | ||
</ref> | </ref> |