Crystal structure of the endogenous agonist-bound prostanoid receptor EP3

Nat Chem Biol. 2019 Jan;15(1):8-10. doi: 10.1038/s41589-018-0171-8. Epub 2018 Dec 3.

Abstract

Prostanoids are a series of bioactive lipid metabolites that function in an autacoid manner via activation of cognate G-protein-coupled receptors (GPCRs). Here, we report the crystal structure of human prostaglandin (PG) E receptor subtype EP3 bound to endogenous ligand PGE2 at 2.90 Å resolution. The structure reveals important insights into the activation mechanism of prostanoid receptors and provides a molecular basis for the binding modes of endogenous ligands.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Crystallography, X-Ray
  • Dinoprostone / chemistry
  • Dinoprostone / metabolism
  • Humans
  • Models, Molecular
  • Protein Conformation
  • Receptors, Prostaglandin E, EP3 Subtype / agonists*
  • Receptors, Prostaglandin E, EP3 Subtype / chemistry*
  • Receptors, Prostaglandin E, EP3 Subtype / genetics
  • Receptors, Prostaglandin E, EP3 Subtype / metabolism
  • Transforming Growth Factor alpha / metabolism

Substances

  • PTGER3 protein, human
  • Receptors, Prostaglandin E, EP3 Subtype
  • Transforming Growth Factor alpha
  • Dinoprostone