Virtual and biomolecular screening converge on a selective agonist for GPR30

Nat Chem Biol. 2006 Apr;2(4):207-12. doi: 10.1038/nchembio775. Epub 2006 Mar 5.

Abstract

Estrogen is a hormone critical in the development, normal physiology and pathophysiology of numerous human tissues. The effects of estrogen have traditionally been solely ascribed to estrogen receptor alpha (ERalpha) and more recently ERbeta, members of the soluble, nuclear ligand-activated family of transcription factors. We have recently shown that the seven-transmembrane G protein-coupled receptor GPR30 binds estrogen with high affinity and resides in the endoplasmic reticulum, where it activates multiple intracellular signaling pathways. To differentiate between the functions of ERalpha or ERbeta and GPR30, we used a combination of virtual and biomolecular screening to isolate compounds that selectively bind to GPR30. Here we describe the identification of the first GPR30-specific agonist, G-1 (1), capable of activating GPR30 in a complex environment of classical and new estrogen receptors. The development of compounds specific to estrogen receptor family members provides the opportunity to increase our understanding of these receptors and their contribution to estrogen biology.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding, Competitive
  • COS Cells
  • Calcium / metabolism
  • Cell Movement
  • Chlorocebus aethiops
  • Databases as Topic
  • Dose-Response Relationship, Drug
  • Enzyme Activation
  • Estrogen Receptor alpha / metabolism
  • Estrogen Receptor beta / metabolism
  • Humans
  • Ligands
  • Microscopy, Fluorescence
  • Models, Biological
  • Models, Molecular
  • Phosphatidylinositol 3-Kinases / metabolism
  • Protein Binding
  • Protein Conformation
  • Receptors, Estrogen / metabolism
  • Receptors, G-Protein-Coupled / agonists*
  • Signal Transduction
  • Time Factors

Substances

  • Estrogen Receptor alpha
  • Estrogen Receptor beta
  • GPER1 protein, human
  • Ligands
  • Receptors, Estrogen
  • Receptors, G-Protein-Coupled
  • Calcium

Associated data

  • PDB/1ERE
  • PDB/3ERT
  • PubChem-Substance/8139852
  • PubChem-Substance/8139853
  • PubChem-Substance/8139854
  • PubChem-Substance/8139855
  • PubChem-Substance/8139856
  • PubChem-Substance/8139857
  • PubChem-Substance/8139858
  • PubChem-Substance/8139859
  • PubChem-Substance/8139860