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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
(actively: E2032, S2035, Y2038, F2039, T2098, W2101, Y2105, F2108, passively: H2028, L2031).  <br />
(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>

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OCA, Dimitri Feltrin, Hamelin Baptiste