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Structure paper

TitleStructural basis of ligand recognition and self-activation of orphan GPR52.
Journal, issue, pagesNature, Vol. 579, Issue 7797, Page 152-157, Year 2020
Publish dateFeb 19, 2020
AuthorsXi Lin / Mingyue Li / Niandong Wang / Yiran Wu / Zhipu Luo / Shimeng Guo / Gye-Won Han / Shaobai Li / Yang Yue / Xiaohu Wei / Xin Xie / Yong Chen / Suwen Zhao / Jian Wu / Ming Lei / Fei Xu /
PubMed AbstractGPR52 is a class-A orphan G-protein-coupled receptor that is highly expressed in the brain and represents a promising therapeutic target for the treatment of Huntington's disease and several ...GPR52 is a class-A orphan G-protein-coupled receptor that is highly expressed in the brain and represents a promising therapeutic target for the treatment of Huntington's disease and several psychiatric disorders. Pathological malfunction of GPR52 signalling occurs primarily through the heterotrimeric G protein, but it is unclear how GPR52 and G couple for signal transduction and whether a native ligand or other activating input is required. Here we present the high-resolution structures of human GPR52 in three states: a ligand-free state, a G-coupled self-activation state and a potential allosteric ligand-bound state. Together, our structures reveal that extracellular loop 2 occupies the orthosteric binding pocket and operates as a built-in agonist, conferring an intrinsically high level of basal activity to GPR52. A fully active state is achieved when G is coupled to GPR52 in the absence of an external agonist. The receptor also features a side pocket for ligand binding. These insights into the structure and function of GPR52 could improve our understanding of other self-activated GPCRs, enable the identification of endogenous and tool ligands, and guide drug discovery efforts that target GPR52.
External linksNature / PubMed:32076264
MethodsEM (single particle) / X-ray diffraction
Resolution2.2 - 3.32 Å
Structure data

0902

6li3

EMDB-0902, PDB-6li3:
cryo-EM structure of GPR52-miniGs-NB35
Method: EM (single particle) / Resolution: 3.32 Å

PDB-6li0:
Crystal structure of GPR52 in complex with agonist c17
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-6li1:
Crystal structure of GPR52 ligand free form with flavodoxin fusion
Method: X-RAY DIFFRACTION / Resolution: 2.9 Å

PDB-6li2:
Crystal structure of GPR52 ligand free form with rubredoxin fusion
Method: X-RAY DIFFRACTION / Resolution: 2.8 Å

Chemicals

ChemComp-EN6:
N-(2-hydroxyethyl)-5-(hydroxymethyl)-3-methyl-1-[2-[[3-(trifluoromethyl)phenyl]methyl]-1-benzothiophen-7-yl]pyrazole-4-carboxamide

ChemComp-FMN:
FLAVIN MONONUCLEOTIDE

ChemComp-OLC:
(2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate

ChemComp-PEG:
DI(HYDROXYETHYL)ETHER

ChemComp-FLC:
CITRATE ANION

ChemComp-HOH:
WATER

ChemComp-PGE:
TRIETHYLENE GLYCOL

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
  • lama glama (llama)
  • desulfovibrio vulgaris str. hildenborough (bacteria)
  • clostridium pasteurianum (bacteria)
KeywordsMEMBRANE PROTEIN / Human GPR52 receptor / Class A / orphan GPCR / agonist c17 / flavodoxin / LCP / apo form / rubredoxin / G-protein coupled receptor / self-activation / cryo-EM

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