6gdg
Cryo-EM structure of the adenosine A2A receptor bound to a miniGs heterotrimer
Structural highlights
FunctionTHIO_ECOLI Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions.AA2AR_HUMAN Receptor for adenosine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Publication Abstract from PubMedThe adenosine A2A receptor (A2AR) is a prototypical G protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein GS. Here we determine the structure by electron cryo-microscopy (cryo-EM) of A2AR at pH 7.5 bound to the small molecule agonist NECA and coupled to an engineered heterotrimeric G protein, which contains mini-GS, the betagamma subunits and nanobody Nb35. Most regions of the complex have a resolution of ~3.8 A or better. Comparison with the 3.4 A resolution crystal structure shows that the receptor and mini-GS 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 beta subunit of the G protein was observed. Cryo-EM structure of the adenosine A2A receptor coupled to an engineered heterotrimeric G protein.,Garcia-Nafria J, Lee Y, Bai X, Carpenter B, Tate CG Elife. 2018 May 4;7. pii: 35946. doi: 10.7554/eLife.35946. PMID:29726815[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
| ||||||||||||||||
