Sandbox Reserved 1177

Figure Legend

NTSR1-ELF, Rattus norvegicus

spinqualitylabelsall models Caption for this structure Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D This is a default text for your page Danny Cotter/Sandbox 1. Click above on edit this page to modify. Be careful with the < and > signs. You may include any references to papers as in: the use of JSmol in Proteopedia or to the article describing Jmol to the rescue. Pymol Pictures Na+ Binding Pocket W321, which is positioned at the bottom of the hydrophobic pocket(green link from allie), sets the top of the Na+ Binding Pocket. The Na+ ion binding pocket acts as a negative allosteric site for G protein activity. When Na+ enters the Na+ ion binding pocket, it coordinates with Asp95, Gln131, and S135, and shuts down the activity of the protein. When the G protein is in its active state, the Na+ ion binding pocket is collapsed, preventing the entrance of Na+. In this case, the Na+ ion is coordinated by a salt bridge to Asp113. The side chain atoms of Asp113 form a hydrogen bond network with Thr156, Ser361, Ser362, and Gln365, which prevents the coordination of a Na+ ion. Neurotensin (Ligand) NTS(8-13). Structural highlights This is a sample scene created with SAT to color by Group, and another to make a transparent representation of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.