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TitleStructural insight into the self-activation and G-protein coupling of P2Y2 receptor.
Journal, issue, pagesCell Discov, Vol. 11, Issue 1, Page 47, Year 2025
Publish dateMay 13, 2025
AuthorsBaoliang Lan / Shuhao Zhang / Kai Chen / Shengjie Dai / Jiaqi Fei / Kaixuan Gao / Xiaoou Sun / Bin Lin / Xiangyu Liu /
PubMed AbstractPurinergic P2Y2 receptor (P2Y2R) represents a typically extracellular ATP and UTP sensor for mediating purinergic signaling. Despite its importance as a pharmacological target, the molecular ...Purinergic P2Y2 receptor (P2Y2R) represents a typically extracellular ATP and UTP sensor for mediating purinergic signaling. Despite its importance as a pharmacological target, the molecular mechanisms underlying ligand recognition and G-protein coupling have remained elusive due to lack of structural information. In this study, we determined the cryo-electron microscopy (cryo-EM) structures of the apo P2Y2R in complex with G, ATP-bound P2Y2R in complex with G or G, and UTP-bound P2Y4R in complex with G. These structures reveal the similarities and distinctions of ligand recognition within the P2Y receptor family. Furthermore, a comprehensive analysis of G-protein coupling reveals that P2Y2R exhibits promiscuity in coupling with both G and G proteins. Combining molecular dynamics simulations and signaling assays, we elucidate the molecular mechanisms by which P2Y2R differentiates pathway-specific G or G coupling through distinct structural components on the intracellular side. Strikingly, we identify a helix-like segment within the N-terminus that occupies the orthosteric ligand-binding pocket of P2Y2R, accounting for its self-activation. Taken together, these findings provide a molecular framework for understanding the activation mechanism of P2Y2R, encompassing ligand recognition, G-protein coupling, and a novel N-terminus-mediated self-activation mechanism.
External linksCell Discov / PubMed:40360475 / PubMed Central
MethodsEM (single particle)
Resolution2.65 - 3.31 Å
Structure data

61947

9k0k

EMDB-61947, PDB-9k0k:
Cryo-EM structure of UTP-bound P2Y purinoceptor 4-miniGq-Nb35 complex
Method: EM (single particle) / Resolution: 3.14 Å

61958

9k0x

EMDB-61958, PDB-9k0x:
Cryo-EM structure of ATP-bound P2Y purinoceptor 2-miniGq-Nb35 complex
Method: EM (single particle) / Resolution: 2.83 Å

61986

9k20

EMDB-61986, PDB-9k20:
Cryo-EM structure of ATP-bound P2Y purinoceptor 2-miniGo-scFv16 complex
Method: EM (single particle) / Resolution: 2.65 Å

61990

9k25

EMDB-61990, PDB-9k25:
Cryo-EM structure of apo-P2Y purinoceptor 2-miniGq-Nb35 complex
Method: EM (single particle) / Resolution: 3.31 Å

Chemicals

ChemComp-UTP:
URIDINE 5'-TRIPHOSPHATE / UTP*YM

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • homo sapiens (human)
  • vicugna pacos (alpaca)
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / G protein-coupled receptors / G-protein signaling / Nucleotide receptors

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