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TitleStructural and dynamic insights into agonist recognition and function of the thromboxane A receptor.
Journal, issue, pagesNat Commun, Year 2026
Publish dateFeb 23, 2026
AuthorsPawel Krawinski / Donna Matzov / Aoife Ryder / Kanhaya Lal / Dmitry S Karlov / Georges Chalhoub / Eamon P Mulvaney / B Therese Kinsella / Peter J McCormick / Martin Caffrey / Irina G Tikhonova / Moran Shalev-Benami /
PubMed AbstractThe thromboxane A receptor (TP), expressed in platelets and smooth muscle, plays an important role in blood clotting and muscle contraction. The endogenous ligand of this G protein-coupled receptor ...The thromboxane A receptor (TP), expressed in platelets and smooth muscle, plays an important role in blood clotting and muscle contraction. The endogenous ligand of this G protein-coupled receptor (GPCR), thromboxane A (TXA), is a short-lived arachidonic acid metabolite with a half-life of ∼30 seconds, which makes investigating the TP structure and activation mechanism highly challenging. Here we determine the structures of the TP in complex with the synthetic agonists, U46619 and I-BOP, stable analogues of the natural ligand, in the presence of the signalling protein partner, G. The structures reveal a unique activation switch for the receptor that differs from typical class A GPCR family members. Complemented by functional studies, mutational analysis, docking, and molecular dynamics (MD) simulations, our investigation highlights the differences between agonist and antagonist binding and explores the ligand entry mechanism to the binding pocket from within the membrane via a molecular gate composed of two transmembrane helices. In addition, our study provides crucial information to aid in the rational design of compounds targeting the TP, and offers mechanistic insights into inherited disorders associated with mutations in the TP.
External linksNat Commun / PubMed:41730883
MethodsEM (single particle)
Resolution3.22 - 3.52 Å
Structure data

51324

9gg5

EMDB-51324, PDB-9gg5:
Cryo-EM structure of Thromboxane A2 receptor-miniGq protein complex bound to U46619
Method: EM (single particle) / Resolution: 3.26 Å

51331

9ggg

EMDB-51331, PDB-9ggg:
Cryo-EM structure of Thromboxane A2 receptor-miniGq Protein Complex bound to I-BOP
Method: EM (single particle) / Resolution: 3.25 Å

EMDB-51332: Consensus cryo-EM map of Thromboxane A2 receptor-Gq Protein Complex bound to U46619
Method: EM (single particle) / Resolution: 3.26 Å

EMDB-51341: Cryo-EM map of Thromboxane A2 receptor-Gq Protein Complex bound to U46619 focused refined on the receptor
Method: EM (single particle) / Resolution: 3.26 Å

EMDB-51342: Cryo-EM map of Thromboxane A2 receptor-Gq Protein Complex bound to U46619 focused refined on the G proteins
Method: EM (single particle) / Resolution: 3.26 Å

EMDB-51343: Cryo-EM map of Thromboxane A2 receptor-Gq Protein Complex bound to IBOP
Method: EM (single particle) / Resolution: 3.25 Å

EMDB-51344: Cryo-EM map of Thromboxane A2 receptor-Gq Protein Complex bound to I-BOP focused refined on the receptor
Method: EM (single particle) / Resolution: 3.52 Å

EMDB-51345: Cryo-EM map of Thromboxane A2 receptor-Gq Protein Complex bound to I-BOP focused refined on the G proteins
Method: EM (single particle) / Resolution: 3.22 Å

Chemicals

ChemComp-PUC:
(5Z)-7-{(1R,4S,5S,6R)-6-[(1E,3S)-3-hydroxyoct-1-en-1-yl]-2-oxabicyclo[2.2.1]hept-5-yl}hept-5-enoic acid

ChemComp-CLR:
CHOLESTEROL

PDB-1ik0:
Solution Structure of Human IL-13

Source
  • homo sapiens (human)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / Single particle cryo-EM / GPCR / G-proteins

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