Sandbox Reserved 1703: Difference between revisions

Line 36:

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

The PAM induced downward shift of helix IV 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 hook-like region ~~(figure 4)~~, from the last 4 terminals of the α-subunit of the G-protein, to move in adjacent to helix IV in the transmembrane domain. Within this interaction, <scene name='90/904308/Binding_site/4'>C351</scene> on the hook participates in hydrophobic interactions with Intracellular loop 2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the shallow groove formed by intracellular loops 2 and 3 and residues on helices 3 and lV<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 resulting in a tighter form. The TMD helices are also reoriented in both monomers to form an asymmetric dimer interface.

The PAM induced downward shift of helix IV 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 the last 4 terminals of the α-subunit of the G-protein, to move in adjacent to helix IV in the transmembrane domain. Within this interaction, <scene name='90/904308/Binding_site/4'>C351</scene> on the hook participates in hydrophobic interactions with Intracellular loop 2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the shallow groove formed by intracellular loops 2 and 3 and residues on helices 3 and lV<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 resulting in a tighter form. The TMD helices are also reoriented in both monomers to form an asymmetric dimer interface.

==Clinical Relevance==

Sandbox Reserved 1703: Difference between revisions

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 36: / Line 36: @@
 ====G-protein Binding====
-The PAM induced downward shift of helix IV 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 hook-like region (figure 4), from the last 4 terminals of the α-subunit of the G-protein, to move in adjacent to helix IV in the transmembrane domain. Within this interaction, <scene name='90/904308/Binding_site/4'>C351</scene> on the hook participates in hydrophobic interactions with Intracellular loop 2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the shallow groove formed by intracellular loops 2 and 3 and residues on helices 3 and lV<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 resulting in a tighter form. The TMD helices are also reoriented in both monomers to form an asymmetric dimer interface.
+The PAM induced downward shift of helix IV 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 the last 4 terminals of the α-subunit of the G-protein, to move in adjacent to helix IV in the transmembrane domain. Within this interaction, <scene name='90/904308/Binding_site/4'>C351</scene> on the hook participates in hydrophobic interactions with Intracellular loop 2 and helix 4. These interactions allow the C-terminal region of the G-protein α-subunit to bind in the shallow groove formed by intracellular loops 2 and 3 and residues on helices 3 and lV<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 resulting in a tighter form. The TMD helices are also reoriented in both monomers to form an asymmetric dimer interface.
 ==Clinical Relevance==