Sandbox Reserved 1703: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 14: | Line 14: | ||
[[Image:Domains of mGlu2.jpg|250 px|right|thumb|'''Figure 2.'''Shown above the line is the intracellular region containing the VFT and CRD. Shown below the line is the extracellular region containing the TMD of mGlu2.]] | [[Image:Domains of mGlu2.jpg|250 px|right|thumb|'''Figure 2.'''Shown above the line is the intracellular region containing the VFT and CRD. Shown below the line is the extracellular region containing the TMD of mGlu2.]] | ||
mGlu2 is a [https://en.wikipedia.org/wiki/Protein_dimer homodimer]. Dimerization of mGlu2 is required to relay glutamate binding from the ECD to its TMD. The homodimer of mGlu2 contains an <scene name='90/904308/Alphaandbetachain/ | mGlu2 is a [https://en.wikipedia.org/wiki/Protein_dimer homodimer]. Dimerization of mGlu2 is required to relay glutamate binding from the ECD to its TMD. The homodimer of mGlu2 contains an <scene name='90/904308/Alphaandbetachain/9'>α-chain and a β-chain</scene>. Occupation of both ECDs with the agonist, glutamate, is necessary for a fully active mGlu2<ref name="Du">Du, Juan, et al. “Structures of Human mglu2 and mglu7 Homo- and Heterodimers.” Nature News, Nature Publishing Group, 16 June 2021, https://www.nature.com/articles/s41586-021-03641-w.></ref>. However, only one chain in the dimer is responsible for activation of the G-protein, this suggests an asymmetrical signal transduction mechanism for mGlu2<ref name="Lin"/>. | ||
Due to conformational changes, mGlu2 moves between different states: inactive, intermediate, PAM bound, and active (Figure 3). | Due to conformational changes, mGlu2 moves between different states: inactive, intermediate, PAM bound, and active (Figure 3). | ||
