In silico design of novel probes for the atypical opioid receptor MRGPRX2

  • Katherine Lansu
  • , Joel Karpiak
  • , Jing Liu
  • , Xi Ping Huang
  • , John D. McCorvy
  • , Wesley K. Kroeze
  • , Tao Che
  • , Hiroshi Nagase
  • , Frank I. Carroll
  • , Jian Jin
  • , Brian K. Shoichet
  • , Bryan L. Roth

Research output: Contribution to journalArticlepeer-review

245 Scopus citations

Abstract

The primate-exclusive MRGPRX2 G protein-coupled receptor (GPCR) has been suggested to modulate pain and itch. Despite putative peptide and small-molecule MRGPRX2 agonists, selective nanomolar-potency probes have not yet been reported. To identify a MRGPRX2 probe, we first screened 5,695 small molecules and found that many opioid compounds activated MRGPRX2, including (-)- and (+)-morphine, hydrocodone, sinomenine, dextromethorphan, and the prodynorphin-derived peptides dynorphin A, dynorphin B, and α- and β-neoendorphin. We used these to select for mutagenesis-validated homology models and docked almost 4 million small molecules. From this docking, we predicted ZINC-3573 - a potent MRGPRX2-selective agonist, showing little activity against 315 other GPCRs and 97 representative kinases - along with an essentially inactive enantiomer. ZINC-3573 activates endogenous MRGPRX2 in a human mast cell line, inducing degranulation and calcium release. MRGPRX2 is a unique atypical opioid-like receptor important for modulating mast cell degranulation, which can now be specifically modulated with ZINC-3573.

Original languageEnglish
Pages (from-to)529-536
Number of pages8
JournalNature Chemical Biology
Volume13
Issue number5
DOIs
StatePublished - May 1 2017

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