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TitleStructural insights into the selective recognition of RF-amide peptides by neuropeptide FF receptor 2.
Journal, issue, pagesEMBO Rep, Year 2025
Publish dateMar 24, 2025
AuthorsJeesoo Kim / Sooyoung Hong / Hajin Lee / Hyun Sik Lee / Chaehee Park / Jinuk Kim / Wonpil Im / Hee-Jung Choi /
PubMed AbstractNeuropeptide FF Receptor 2 (NPFFR2), a G-protein-coupled receptor, plays a role in pain modulation and diet-induced thermogenesis. While NPFFR2 is strongly activated by neuropeptides FF (NPFFs), it ...Neuropeptide FF Receptor 2 (NPFFR2), a G-protein-coupled receptor, plays a role in pain modulation and diet-induced thermogenesis. While NPFFR2 is strongly activated by neuropeptides FF (NPFFs), it shows low activity in response to RF-amide-related peptides (RFRPs), despite the peptides belonging to a shared family. In contrast, NPFFR1, which shares high sequence similarity with NPFFR2, is activated by RFRPs and regulates reproductive hormone balance. The molecular basis for these receptor-specific interactions with their RF-amide peptides remains unclear. Here, we present cryo-electron microscopy structures of NPFFR2 in its active state bound to the agonist RF-amide peptide hNPSF, and in its ligand-free state. Structural analysis reveals that the C-terminal RF-amide moiety engages conserved residues in the transmembrane domain, while the N-terminal segment interacts in a receptor subtype-specific manner. Key selectivity-determining residues in NPFFR2 are also identified. A homology model of NPFFR1 bound to RFRP, supported by mutagenesis studies, further validates this selectivity mechanism. Additionally, structural comparison between the inactive and active states of NPFFR2 suggests a TM3-mediated activation mechanism. These findings provide insights into RF-amide peptide recognition by NPFF receptors.
External linksEMBO Rep / PubMed:40128413
MethodsEM (single particle)
Resolution2.91 - 3.21 Å
Structure data

61444

9jfy

EMDB-61444, PDB-9jfy:
Cryo-EM structure of Neuropeptide FF receptor 2 in complex with hNPSF and Gi
Method: EM (single particle) / Resolution: 3.21 Å

61446

9jg0

EMDB-61446, PDB-9jg0:
Cryo-EM structure of neuropeptide FF receptor 2 in the ligand-free state with BRIL fusion, anti-BRIL Fab, and nanobody
Method: EM (single particle) / Resolution: 2.91 Å

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • synthetic construct (others)
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / GPCR / G-protein / neuropeptide

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