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TitleDivergent activation patterns of BRS3 revealed by two Chinese herb-derived agonists.
Journal, issue, pagesActa Pharm Sin B, Vol. 15, Issue 10, Page 5231-5243, Year 2025
Publish dateJun 30, 2025
AuthorsJie Li / Changyao Li / Qingtong Zhou / Wei Han / Mingzhu Fang / Youwei Xu / Yiting Mai / Yao Zhang / Jiahua Cui / H Eric Xu / Yan Zhang / Wanchao Yin / Ming-Wei Wang /
PubMed AbstractBombesin receptor subtype-3 (BRS3) is an orphan G protein-coupled receptor (GPCR) that plays critical roles in energy homeostasis, glucose metabolism, and insulin secretion. Recent structural studies ...Bombesin receptor subtype-3 (BRS3) is an orphan G protein-coupled receptor (GPCR) that plays critical roles in energy homeostasis, glucose metabolism, and insulin secretion. Recent structural studies have elucidated BRS3 signaling mechanisms using synthetic ligands, including BA1 and MK-5046. However, the molecular basis of BRS3 activation by bioactive natural compounds and their derivatives, particularly those derived from traditional Chinese medicine, remains unclear. Here, we present high-resolution cryogenic electron microscopy (cryo-EM) structures of the human BRS3-G complex in both unliganded and active states bound by two herb-derived compounds (DSO-5a and oridonin), at resolutions of 2.9, 2.8, and 2.9 Å, respectively. These structures display distinct ligand recognition patterns between DSO-5a and oridonin. Although both compounds bind to the orthosteric pocket, they differentially engage the interaction network of BRS3, as demonstrated by mutagenesis studies assessing calcium mobilization and inositol phosphate 1 (IP1) accumulation. These findings enhance our understanding of BRS3 activation and provide valuable insights into the development of small-molecule BRS3 modulators with therapeutic potential.
External linksActa Pharm Sin B / PubMed:41132856 / PubMed Central
MethodsEM (single particle)
Resolution2.83 - 2.93 Å
Structure data

61941

9k07

EMDB-61941, PDB-9k07:
Cryo-EM structure of the DSO-5a-bound human BRS3-Gq complex
Method: EM (single particle) / Resolution: 2.83 Å

63455

9lwp

EMDB-63455, PDB-9lwp:
Cryo-EM structure of the unliganded human BRS3-Gq complex
Method: EM (single particle) / Resolution: 2.93 Å

Chemicals

PDB-1el6:
STRUCTURE OF BACTERIOPHAGE T4 GENE PRODUCT 11, THE INTERFACE BETWEEN THE BASEPLATE AND SHORT TAIL FIBERS

Source
  • homo sapiens (human)
  • oplophorus gracilirostris (crustacean)
  • mus musculus (house mouse)
  • rattus norvegicus (Norway rat)
  • bos taurus (domestic cattle)
  • lama glama (llama)
KeywordsMEMBRANE PROTEIN / DSO-5a / Unliganded

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