Sandbox Reserved 1703: Difference between revisions

[https://en.wikipedia.org/wiki/Cryogenic_electron_microscopy Cryo-EM] studies of mGlu2 have yielded adequate structural maps of mGlu2 in various activation states. These maps provided clearer understanding of the conformational changes between the inactive and active states of mGlu2<ref name="Lin" />. The conformational changes allow mGlu2 to move from an inactive <scene name='90/904307/Inactive_to_active_morph/1'>open to a closed</scene> active conformation. The overall <scene name='90/904307/Inactive_structure/1'>structure</scene> of the mGlu2 is composed of 3 main parts. First, a ligand binding <scene name='90/904307/Better_inactive_structure/3'>Venus Fly Trap Domain(VFT)</scene>, that binds two glutamates which are the agonists. This is followed by a <scene name='90/904307/Better_inactive_structure/2'>Cysteine Rich Domain(CRD)</scene> that links the VFT to the TMD. The CRD is helpful in relaying signals for conformational changes in the TMD induced by agonist binding in the VFT<ref name="Lin" />. The VFT and CRD are located in the intracellular domain(ICD), while the TMD is located in the ECD (Figure 2). Finally the <scene name='90/904307/Better_inactive_structure/4'>TMD</scene> contains 7 α-helices (7TM) on both the α and β chains. The TMD aids in the binding of the G-protein.