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| Title | Cryo-EM structure of the adenosine A receptor coupled to an engineered heterotrimeric G protein. |
|---|---|
| Journal, issue, pages | Elife, Vol. 7, Year 2018 |
| Publish date | May 4, 2018 |
 Authors | Javier García-Nafría / Yang Lee / Xiaochen Bai / Byron Carpenter / Christopher G Tate /  |
| PubMed Abstract | The adenosine A receptor (AR) is a prototypical G protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein G. Here, we determine the structure by electron cryo-microscopy (cryo-EM) ...The adenosine A receptor (AR) is a prototypical G protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein G. Here, we determine the structure by electron cryo-microscopy (cryo-EM) of AR at pH 7.5 bound to the small molecule agonist NECA and coupled to an engineered heterotrimeric G protein, which contains mini-G, the βγ subunits and nanobody Nb35. Most regions of the complex have a resolution of ~3.8 Å or better. Comparison with the 3.4 Å resolution crystal structure shows that the receptor and mini-G are virtually identical and that the density of the side chains and ligand are of comparable quality. However, the cryo-EM density map also indicates regions that are flexible in comparison to the crystal structures, which unexpectedly includes regions in the ligand binding pocket. In addition, an interaction between intracellular loop 1 of the receptor and the β subunit of the G protein was observed. |
 External links | Elife / PubMed:29726815 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 4.11 Å |
| Structure data | |
| Chemicals |  ChemComp-NEC: |
| Source |
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 Keywords | MEMBRANE PROTEIN / G-protein coupled receptor / adenosine / GPCR / A2A receptor |
escherichia coli (E. coli)
homo sapiens (human)
lama glama (llama)