Sandbox Reserved 1703: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

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 ====G-Protein Recognition====
- Reorientation positions helix lll on either the alpha or beta chain because both have the ability to bind to the G-protein but only one chain is required for full receptor activation. The intracellular region of helix lll mainly contributes to the interactions with the alpha subunit of the G-protein. Intracellular Loop 2 plays a key role in G-protein coupling as well by building polar interaction networks through its ionic interactions with the alpha subunit of the G-protein. Lastly, mGlu2 residue E666 forms a salt bridge with an alpha N residue (R32) on the alpha subunit which further destabilizes the inactive conformation<ref name="Lin"/>.
+Reorientation positions helix lll on either the alpha or beta chain because both have the ability to bind to the G-protein but only one chain is required for full receptor activation. The intracellular region of helix lll mainly contributes to the interactions with the alpha subunit of the G-protein. Intracellular Loop 2 plays a key role in G-protein coupling as well by building polar interaction networks through its ionic interactions with the alpha subunit of the G-protein. Lastly, mGlu2 residue E666 forms a salt bridge with an alpha N residue (R32) on the alpha subunit which further destabilizes the inactive conformation<ref name="Lin"/>.
 ====G-protein Binding====