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TitleStructural basis of adhesion GPCR GPR110 activation by stalk peptide and G-proteins coupling.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5513, Year 2022
Publish dateSep 20, 2022
AuthorsXinyan Zhu / Yu Qian / Xiaowan Li / Zhenmei Xu / Ruixue Xia / Na Wang / Jiale Liang / Han Yin / Anqi Zhang / Changyou Guo / Guangfu Wang / Yuanzheng He /
PubMed AbstractAdhesion G protein-coupled receptors (aGPCRs) are keys of many physiological events and attractive targets for various diseases. aGPCRs are also known to be capable of self-activation via an ...Adhesion G protein-coupled receptors (aGPCRs) are keys of many physiological events and attractive targets for various diseases. aGPCRs are also known to be capable of self-activation via an autoproteolysis process that removes the inhibitory GAIN domain on the extracellular side of receptor and releases a stalk peptide to bind and activate the transmembrane side of receptor. However, the detailed mechanism of aGPCR activation remains elusive. Here, we report the cryo-electron microscopy structures of GPR110 (ADGRF1), a member of aGPCR, in complex with G, G, G, G and G The structures reveal distinctive ligand engaging model and activation conformations of GPR110. The structures also unveil the rarely explored GPCR/G and GPCR/G engagements. A comparison of G, G, G, G and G engagements with GPR110 reveals details of G-protein engagement, including a dividing point at the far end of the alpha helix 5 (αH5) of Gα subunit that separates G/G engagements from G/G/G engagements. This is also where G/G bind the receptor through both hydrophobic and polar interaction, while G/G/G engage receptor mainly through hydrophobic interaction. We further provide physiological evidence of GPR110 activation via stalk peptide. Taken together, our study fills the missing information of GPCR/G-protein engagement and provides a framework for understanding aGPCR activation and GPR110 signaling.
External linksNat Commun / PubMed:36127364 / PubMed Central
MethodsEM (single particle)
Resolution2.83 - 3.09 Å
Structure data

32881

7wxu

EMDB-32881: Protein 110 and Q complex
PDB-7wxu: GPR110/Gq complex
Method: EM (single particle) / Resolution: 2.85 Å

32882

7wxw

EMDB-32882: Protein 110 and S complex
PDB-7wxw: GPR110/Gs complex
Method: EM (single particle) / Resolution: 2.84 Å

32883

7wy0

EMDB-32883: Protein 110 and 13 complex
PDB-7wy0: GPR110/G13 complex
Method: EM (single particle) / Resolution: 2.83 Å

32905

7wz7

EMDB-32905: Protein 110 and 12 complex
PDB-7wz7: GPR110/G12 complex
Method: EM (single particle) / Resolution: 2.83 Å

32972

7x2v

EMDB-32972: Protein 110 and i complex
PDB-7x2v: GPR110/Gi complex
Method: EM (single particle) / Resolution: 3.09 Å

Source
  • homo sapiens (human)
  • lama glama (llama)
KeywordsMEMBRANE PROTEIN / GPCR

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