Sandbox Reserved 1715: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 59: | Line 59: | ||
=== Conformational Changes === | === Conformational Changes === | ||
'''1.''' mGlu starts in an <scene name='90/904320/inactive homodimeric form/2'>Inactive mGlu</scene>. In this conformation, the receptor is considered open with an inter-lobe angle of 44 degrees.The structure has two free binding sites in the VFT, the CRDs are separated, and the TMD is not interacting with a G protein. [[Image: Protein Interaction with G Protein.png| | '''1.''' mGlu starts in an <scene name='90/904320/inactive homodimeric form/2'>Inactive mGlu</scene>. In this conformation, the receptor is considered open with an inter-lobe angle of 44 degrees.The structure has two free binding sites in the VFT, the CRDs are separated, and the TMD is not interacting with a G protein. [[Image: Protein Interaction with G Protein.png|400 px|right|thumb|Figure 1. The interaction between an active mGlu and a G-protein ]] | ||
'''2.''' In the intermediate activation state (known as the open-closed conformation), one glutamate is bound in one binding pocket of VFT. This state is still considered inactive as the receptor has not changed the conformations in the CRD and thus the TMD. With the same asymmetric transmembrane helices formation, a TM3-TM4 interface is still present and mGlu cannot interact with a G protein. (IMAGE) | '''2.''' In the intermediate activation state (known as the open-closed conformation), one glutamate is bound in one binding pocket of VFT. This state is still considered inactive as the receptor has not changed the conformations in the CRD and thus the TMD. With the same asymmetric transmembrane helices formation, a TM3-TM4 interface is still present and mGlu cannot interact with a G protein. (IMAGE) | ||