Sandbox Reserved 825: Difference between revisions
| Line 49: | Line 49: | ||
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> | binding. <ref> PMCID: PMC2698317 </ref> | ||
[[Image:FRB HTS-1 Rapamycin.png|center|upright=2| thumb| Fig.3 A representative view of the mTOR inhibitor HTS-1 docked into its binding site on the FRB domain on the left. On the right, the location and conformation of rapamycin bound to the FRB domain in the ternary complex formed with FKBP12 is illustrated, with the domain shown in the same orientation as on the left.]] | [[Image:FRB HTS-1 Rapamycin.png|center|upright=2| thumb| Fig.3 A representative view of the mTOR inhibitor HTS-1 docked into its binding site on the FRB domain on the left. On the right, the location and conformation of rapamycin bound to the FRB domain in the ternary complex formed with FKBP12 is illustrated, with the domain shown in the same orientation as on the left.]] | ||