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TitleDeciphering molecular determinants of GPBAR1-Gs protein interactions by HDX-MS and cryo-EM.
Journal, issue, pagesSci Rep, Vol. 15, Issue 1, Page 31517, Year 2025
Publish dateAug 26, 2025
AuthorsJérôme Castel / Thomas Botzanowski / Ieva Brooks / Alexandre Frechard / Gilbert Bey / Marine Schroeter / Elise Del Nero / François Debaene / Fabrice Ciesielski / Denis Zeyer / Sarah Cianferani / Renaud Morales /
PubMed AbstractMany physiological processes are dependent on G protein-coupled receptors (GPCRs), the biggest family of human membrane proteins and a significant class of therapeutic targets. Once activated by ...Many physiological processes are dependent on G protein-coupled receptors (GPCRs), the biggest family of human membrane proteins and a significant class of therapeutic targets. Once activated by external stimuli, GPCRs use G proteins and arrestins as transducers to generate second messengers and trigger downstream signaling, leading to diverse signaling profiles. The G protein-coupled bile acid receptor 1 (GPBAR1, also known as Takeda G protein-coupled receptor 5, TGR5) is a class A bile acid membrane receptor that regulates energy homeostasis and glucose and lipid metabolism. GPBAR1/Gs protein interactions are implicated in the prevention of diabetes and the reduction of inflammatory responses, making GPBAR1 a potential therapeutic target for metabolic disorders. Here, we present combined hydrogen/deuterium exchange mass spectrometry (HDX-MS) and cryo-electron microscopy (cryo-EM) to identify the molecular determinants of GPBAR1 conformational dynamics upon G protein binding. Thanks to extensive optimization, we achieved over 75% sequence coverage by HDX-MS of a complete GPCR complex and a 2.5 Å resolution structure by cryo-EM, both of which are state-of-the-art. Altogether, our results provide information on the under-investigated GPBAR1 binding mode to its cognate G protein, pinpointing the synergic and powerful combination of higher cryo-EM and lower HDX-MS resolution techniques to dissect GPCR/G protein binding characteristics.
External linksSci Rep / PubMed:40858717 / PubMed Central
MethodsEM (single particle)
Resolution2.5 Å
Structure data

51700

9gyo

EMDB-51700, PDB-9gyo:
CryoEM structure of Gs-coupled GPBAR with small molecule agonist P395
Method: EM (single particle) / Resolution: 2.5 Å

Chemicals

ChemComp-FWX:
2-(ethylamino)-6-[3-(4-propan-2-ylphenyl)propanoyl]-7,8-dihydro-5H-pyrido[4,3-d]pyrimidine-4-carboxamide

ChemComp-CLR:
CHOLESTEROL

Source
  • homo sapiens (human)
  • lama glama (llama)
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / G-protein coupled receptor / transmembrane protein / G protein signaling / bile acid-binding.

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