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TitleStructures of the glucocorticoid-bound adhesion receptor GPR97-G complex.
Journal, issue, pagesNature, Vol. 589, Issue 7843, Page 620-626, Year 2021
Publish dateJan 6, 2021
AuthorsYu-Qi Ping / Chunyou Mao / Peng Xiao / Ru-Jia Zhao / Yi Jiang / Zhao Yang / Wen-Tao An / Dan-Dan Shen / Fan Yang / Huibing Zhang / Changxiu Qu / Qingya Shen / Caiping Tian / Zi-Jian Li / Shaolong Li / Guang-Yu Wang / Xiaona Tao / Xin Wen / Ya-Ni Zhong / Jing Yang / Fan Yi / Xiao Yu / H Eric Xu / Yan Zhang / Jin-Peng Sun /
PubMed AbstractAdhesion G-protein-coupled receptors (GPCRs) are a major family of GPCRs, but limited knowledge of their ligand regulation or structure is available. Here we report that glucocorticoid stress ...Adhesion G-protein-coupled receptors (GPCRs) are a major family of GPCRs, but limited knowledge of their ligand regulation or structure is available. Here we report that glucocorticoid stress hormones activate adhesion G-protein-coupled receptor G3 (ADGRG3; also known as GPR97), a prototypical adhesion GPCR. The cryo-electron microscopy structures of GPR97-G 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, 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 protein, contributing to the high basal activity of GRP97. Palmitoylation at the cytosolic tail of the G 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.
External linksNature / PubMed:33408414
MethodsEM (single particle)
Resolution2.9 - 3.1 Å
Structure data

30602

7d76

EMDB-30602, PDB-7d76:
Cryo-EM structure of the beclomethasone-bound adhesion receptor GPR97-Go complex
Method: EM (single particle) / Resolution: 3.1 Å

30603

7d77

EMDB-30603, PDB-7d77:
Cryo-EM structure of the cortisol-bound adhesion receptor GPR97-Go complex
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-GXR:
(8~{S},9~{R},10~{S},11~{S},13~{S},14~{S},16~{S},17~{R})-9-chloranyl-10,13,16-trimethyl-11,17-bis(oxidanyl)-17-(2-oxidanylethanoyl)-6,7,8,11,12,14,15,16-octahydrocyclopenta[a]phenanthren-3-one

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-HCY:
(11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione / medication, hormone*YM / Cortisol

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / GPCR / GPR97 / complex / adhesion G protein-coupled receptor

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