Sandbox Reserved 825: Difference between revisions
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[[Image:FRB Phosphatidic Acid.png|upright=1.25|center|thumb| Fig.2 A representative view of phosphatidic acid docked into its binding site on the FRB domain.]] | [[Image:FRB Phosphatidic Acid.png|upright=1.25|center|thumb| Fig.2 A representative view of phosphatidic acid docked into its binding site on the FRB domain.]] | ||
{{clear}} | {{clear}} | ||
Other molecules like the novel class inhibitor '''HTS-1''' (4-[6-{[(1S,2R)-2-(benzyloxy)cyclopentyl]acety}-4-(2-thienyl)pyridin-2-yl]-4- | Other molecules like the novel class inhibitor '''HTS-1''' (4-[6-{[(1S,2R)-2-(benzyloxy)cyclopentyl]acety}-4-(2-thienyl)pyridin-2-yl]-4-oxobutanoic acid) | ||
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 (actively: E2032, S2035, Y2038, F2039, T2098, W2101, Y2105, F2108, passively: H2028, L2031). 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 (actively: E2032, S2035, Y2038, F2039, T2098, W2101, Y2105, F2108, passively: H2028, L2031). At least <scene name='56/568023/Ovelap_pa_and_hts-1/1'>six</scene> of those residues also take part in phosphatidic acid | ||