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TitleMolecular insights into differentiated ligand recognition of the human parathyroid hormone receptor 2.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 118, Issue 32, Year 2021
Publish dateAug 10, 2021
AuthorsXi Wang / Xi Cheng / Lihua Zhao / Yuzhe Wang / Chenyu Ye / Xinyu Zou / Antao Dai / Zhaotong Cong / Jian Chen / Qingtong Zhou / Tian Xia / Hualiang Jiang / H Eric Xu / Dehua Yang / Ming-Wei Wang /
PubMed AbstractThe parathyroid hormone receptor 2 (PTH2R) is a class B1 G protein-coupled receptor (GPCR) involved in the regulation of calcium transport, nociception mediation, and wound healing. Naturally ...The parathyroid hormone receptor 2 (PTH2R) is a class B1 G protein-coupled receptor (GPCR) involved in the regulation of calcium transport, nociception mediation, and wound healing. Naturally occurring mutations in PTH2R were reported to cause hereditary diseases, including syndromic short stature. Here, we report the cryogenic electron microscopy structure of PTH2R bound to its endogenous ligand, tuberoinfundibular peptide (TIP39), and a heterotrimeric G protein at a global resolution of 2.8 Å. The structure reveals that TIP39 adopts a unique loop conformation at the N terminus and deeply inserts into the orthosteric ligand-binding pocket in the transmembrane domain. Molecular dynamics simulation and site-directed mutagenesis studies uncover the basis of ligand specificity relative to three PTH2R agonists, TIP39, PTH, and PTH-related peptide. We also compare the action of TIP39 with an antagonist lacking six residues from the peptide N terminus, TIP(7-39), which underscores the indispensable role of the N terminus of TIP39 in PTH2R activation. Additionally, we unveil that a disease-associated mutation G258D significantly diminished cAMP accumulation induced by TIP39. Together, these results not only provide structural insights into ligand specificity and receptor activation of class B1 GPCRs but also offer a foundation to systematically rationalize the available pharmacological data to develop therapies for various disorders associated with PTH2R.
External linksProc Natl Acad Sci U S A / PubMed:34353904 / PubMed Central
MethodsEM (single particle)
Resolution2.8 Å
Structure data

31405

7f16

EMDB-31405, PDB-7f16:
Cryo-EM structure of parathyroid hormone receptor type 2 in complex with a tuberoinfundibular peptide of 39 residues and G protein
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

Source
  • homo sapiens (human)
  • rattus norvegicus (Norway rat)
  • bos taurus (cattle)
  • lama glama (llama)
KeywordsSIGNALING PROTEIN / Complex / G protein / GPCR / PTH2R

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