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TitleInsights into G-protein coupling preference from cryo-EM structures of G-bound PTH1R.
Journal, issue, pagesNat Chem Biol, Vol. 21, Issue 12, Page 1906-1914, Year 2025
Publish dateJun 26, 2025
AuthorsFumiya K Sano / Kota Shimizume / Kazuhiro Kobayashi / Toshikuni Awazu / Kouki Kawakami / Hiroaki Akasaka / Takaaki A Kobayashi / Tatsuki Tanaka / Hiroyuki H Okamoto / Hisato Hirano / Tsukasa Kusakizako / Wataru Shihoya / Yoshiaki Kise / Yuzuru Itoh / Ryuichiro Ishitani / Yasushi Okada / Yasushi Sako / Masataka Yanagawa / Asuka Inoue / Osamu Nureki /
PubMed AbstractThe parathyroid hormone type 1 receptor (PTH1R) is a prototypical class B1 G-protein-coupled receptor that couples to both G and G, having a crucial role in calcium homeostasis and serving as a ...The parathyroid hormone type 1 receptor (PTH1R) is a prototypical class B1 G-protein-coupled receptor that couples to both G and G, having a crucial role in calcium homeostasis and serving as a therapeutic target for osteoporosis. Therapies targeting PTH1R face challenges because of G-associated prolonged signaling, which leads to bone resorption. To address this, selective activation of G signaling is desirable. However, the structural basis of G-mediated signaling remains unclear, limiting the development of signal-selective drugs. Here, we present cryo-electron microscopy structures of the PTH1R-G complex in two distinct extracellular conformations, demonstrating the role of N-linked glycans at N176 in stabilizing the ligand-tilted conformation. Comparison with a G-bound PTH1R structure highlights the role of key interactions involving both the C terminus of Gα and the receptor's intracellular loop 2 in G signaling. These structural insights provide a foundation for understanding the molecular mechanisms of PTH1R signaling.
External linksNat Chem Biol / PubMed:40571720 / PubMed Central
MethodsEM (single particle)
Resolution2.75 - 2.8 Å
Structure data

61746

9jr2

EMDB-61746, PDB-9jr2:
Cryo-EM structure of PTH-PTH1R-Gq (upright state)
Method: EM (single particle) / Resolution: 2.8 Å

61747

9jr3

EMDB-61747, PDB-9jr3:
Cryo-EM structure of PTH-PTH1R-Gq (tilted state)
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-61795: Cryo-EM structure of PTH-PTH1R-Gq complex (upright state; consensus refinement)
Method: EM (single particle) / Resolution: 2.76 Å

EMDB-61796: Cryo-EM structure of PTH-PTH1R-Gq complex (upright state; receptor focused refinement)
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-61797: Cryo-EM structure of PTH-PTH1R-Gq complex (tilted state; consensus refinement map)
Method: EM (single particle) / Resolution: 2.77 Å

EMDB-61798: Cryo-EM structure of PTH-PTH1R-Gq complex (tilted state; focused refinement map)
Method: EM (single particle) / Resolution: 2.75 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • rattus rattus (black rat)
  • bos taurus (domestic cattle)
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN/IMMUNE SYSTEM / Class B GPCRs / Gq / PTH / SIGNALING PROTEIN / SIGNALING PROTEIN-IMMUNE SYSTEM complex

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