Sandbox Reserved 1177: Difference between revisions

From Proteopedia
Jump to navigationJump to search
No edit summary
No edit summary
Line 13: Line 13:
===Na+ Binding Pocket===
===Na+ Binding Pocket===


<scene name='72/721548/W321/1'>W321</scene>, which is positioned at the bottom of the hydrophobic pocket(green link from allie), sets the top of the <scene name='72/721548/Na_bind_pocket/12'>Na+ Binding Pocket</scene>. 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.  
<scene name='72/721548/W321/1'>W321</scene>, which is positioned at the bottom of the hydrophobic pocket(green link from allie), sets the top of the <scene name='72/721548/Na_bind_pocket/13'>Na+ Binding Pocket</scene>. 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) ==
== Neurotensin (Ligand) ==