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 overall <scene name='90/904307/Inactive_structure/1'>structure</scene> of the mGlu2 is composed of 3 main parts: a ligand binding <scene name='90/904307/Better_inactive_structure/3'>Venus Fly Trap Domain (VFT)</scene>, followed by a <scene name='90/904307/Better_inactive_structure/2'>Cysteine Rich Domain (CRD)</scene> linker to the <scene name='90/904307/Better_inactive_structure/4'>Transmembrane Domain</scene> that contains 7 α-helices (7TM) on both the α and β chains. The VFT and CRD are located in the intracellular domain (ICD), while the TMD is located in the extracellular domain (ECD) (Figure 2). The TMD aids in the binding of the G-protein.