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 [1] or to the article describing Jmol [2] to the rescue.
Introduction
Neurotensin receptor 1 (NTSR1) is a G-protein coupled receptor (GPCR) that binds to the 13 amino acid peptide, neurotensin. Studies determining the structure of NTSR1 crystallized the GPCR bound with the C-terminus of its tridecapeptide ligand, because
because
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 . 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 regulation of protein activity through a Na+ ion. 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)
.
Function
Disease
Relevance
Structural highlights
This is a sample scene created with SAT to by Group, and another to make of the protein. You can make your own scenes on SAT starting from scratch or loading and editing one of these sample scenes.