Sandbox Reserved 1703: Difference between revisions

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====G-protein Binding====

The PAM induced downward shift of helix 6 coupled with the reorientation of the transmembrane domain to a TM6-TM6 asymmetric interface, opens up a cleft on the intracellular surface of the receptor. This cleft allows a <scene name='90/904308/Hook_region/1'>hook-like region</scene>, from terminal 4 residues of the α-subunit of the G-protein to move in adjacent to helix 4 in the TMD. Within this interaction, <scene name='90/904308/Hook_region_recognition/2'>C351</scene> on the hook participates in hydrophobic interactions with ICL2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the cleft formed by ICL2 and residues on helix 4<ref name="Lin" />.The receptor is now <scene name='90/~~904308~~/~~Active_structure~~/3'>fully active</scene> with the dimer coupled only to one G-protein. The VFT is in the closed conformation and the TMD helices are also reoriented in both monomers to form an asymmetric dimer interface. These interactions allow the G-protein to bind which causes mGlu2 to be fully active. Now that mGlu2 is active it can regulate different signaling transductions in the cell<ref name="Lin"/>.

The PAM induced downward shift of helix 6 coupled with the reorientation of the transmembrane domain to a TM6-TM6 asymmetric interface, opens up a cleft on the intracellular surface of the receptor. This cleft allows a <scene name='90/904308/Hook_region/1'>hook-like region</scene>, from terminal 4 residues of the α-subunit of the G-protein to move in adjacent to helix 4 in the TMD. Within this interaction, <scene name='90/904308/Hook_region_recognition/2'>C351</scene> on the hook participates in hydrophobic interactions with ICL2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the cleft formed by ICL2 and residues on helix 4<ref name="Lin" />.The receptor is now <scene name='90/904307/Main_active_image/4'>fully active</scene> with the dimer coupled only to one G-protein. The VFT is in the closed conformation and the TMD helices are also reoriented in both monomers to form an asymmetric dimer interface. These interactions allow the G-protein to bind which causes mGlu2 to be fully active. Now that mGlu2 is active it can regulate different signaling transductions in the cell<ref name="Lin"/>.

==Clinical Relevance==

Sandbox Reserved 1703: Difference between revisions

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 ====G-protein Binding====
-The PAM induced downward shift of helix 6 coupled with the reorientation of the transmembrane domain to a TM6-TM6 asymmetric interface, opens up a cleft on the intracellular surface of the receptor. This cleft allows a <scene name='90/904308/Hook_region/1'>hook-like region</scene>, from terminal 4 residues of the α-subunit of the G-protein to move in adjacent to helix 4 in the TMD. Within this interaction, <scene name='90/904308/Hook_region_recognition/2'>C351</scene> on the hook participates in hydrophobic interactions with ICL2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the cleft formed by ICL2 and residues on helix 4<ref name="Lin" />.The receptor is now <scene name='90/904308/Active_structure/3'>fully active</scene> with the dimer coupled only to one G-protein. The VFT is in the closed conformation and the TMD helices are also reoriented in both monomers to form an asymmetric dimer interface. These interactions allow the G-protein to bind which causes mGlu2 to be fully active. Now that mGlu2 is active it can regulate different signaling transductions in the cell<ref name="Lin"/>.
+The PAM induced downward shift of helix 6 coupled with the reorientation of the transmembrane domain to a TM6-TM6 asymmetric interface, opens up a cleft on the intracellular surface of the receptor. This cleft allows a <scene name='90/904308/Hook_region/1'>hook-like region</scene>, from terminal 4 residues of the α-subunit of the G-protein to move in adjacent to helix 4 in the TMD. Within this interaction, <scene name='90/904308/Hook_region_recognition/2'>C351</scene> on the hook participates in hydrophobic interactions with ICL2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the cleft formed by ICL2 and residues on helix 4<ref name="Lin" />.The receptor is now <scene name='90/904307/Main_active_image/4'>fully active</scene> with the dimer coupled only to one G-protein. The VFT is in the closed conformation and the TMD helices are also reoriented in both monomers to form an asymmetric dimer interface. These interactions allow the G-protein to bind which causes mGlu2 to be fully active. Now that mGlu2 is active it can regulate different signaling transductions in the cell<ref name="Lin"/>.
 ==Clinical Relevance==