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Structures of the glucocorticoid-bound adhesion receptor GPR97–Go complex
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Structures of the glucocorticoid-bound adhesion receptor GPR97–Go complex
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Journal Article
Structures of the glucocorticoid-bound adhesion receptor GPR97–Go complex
2021
Overview
Adhesion G-protein-coupled receptors (GPCRs) are a major family of GPCRs, but limited knowledge of their ligand regulation or structure is available
1
–
3
. Here we report that glucocorticoid stress hormones activate adhesion G-protein-coupled receptor G3 (ADGRG3; also known as GPR97)
4
–
6
, a prototypical adhesion GPCR. The cryo-electron microscopy structures of GPR97–G
o
complexes bound to the anti-inflammatory drug beclomethasone or the steroid hormone cortisol revealed that glucocorticoids bind to a pocket within the transmembrane domain. The steroidal core of glucocorticoids is packed against the ‘toggle switch’ residue W
6.53
, which senses the binding of a ligand and induces activation of the receptor. Active GPR97 uses a quaternary core and HLY motif to fasten the seven-transmembrane bundle and to mediate G protein coupling. The cytoplasmic side of GPR97 has an open cavity, where all three intracellular loops interact with the G
o
protein, contributing to the high basal activity of GRP97. Palmitoylation at the cytosolic tail of the G
o
protein was found to be essential for efficient engagement with GPR97 but is not observed in other solved GPCR complex structures. Our work provides a structural basis for ligand binding to the seven-transmembrane domain of an adhesion GPCR and subsequent G protein coupling.
The authors report on the structure of a glucocorticoid-bound adhesion G-protein-coupled receptor–G protein complex.
