5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology

Yao Peng, John D. McCorvy, Kasper Harpsøe, Katherine Lansu, Shuguang Yuan, Petr Popov, Lu Qu, Mengchen Pu, Tao Che, Louise F. Nikolajsen, Xi Ping Huang, Yiran Wu, Ling Shen, Walden E. Bjørn-Yoshimoto, Kang Ding, Daniel Wacker, Gye Won Han, Jianjun Cheng, Vsevolod Katritch, Anders A. JensenMichael A. Hanson, Suwen Zhao, David E. Gloriam, Bryan L. Roth, Raymond C. Stevens, Zhi Jie Liu

Research output: Contribution to journalArticlepeer-review

183 Scopus citations

Abstract

Drugs frequently require interactions with multiple targets—via a process known as polypharmacology—to achieve their therapeutic actions. Currently, drugs targeting several serotonin receptors, including the 5-HT2C receptor, are useful for treating obesity, drug abuse, and schizophrenia. The competing challenges of developing selective 5-HT2C receptor ligands or creating drugs with a defined polypharmacological profile, especially aimed at G protein-coupled receptors (GPCRs), remain extremely difficult. Here, we solved two structures of the 5-HT2C receptor in complex with the highly promiscuous agonist ergotamine and the 5-HT2A-C receptor-selective inverse agonist ritanserin at resolutions of 3.0 Å and 2.7 Å, respectively. We analyzed their respective binding poses to provide mechanistic insights into their receptor recognition and opposing pharmacological actions. This study investigates the structural basis of polypharmacology at canonical GPCRs and illustrates how understanding characteristic patterns of ligand-receptor interaction and activation may ultimately facilitate drug design at multiple GPCRs. Understanding how one drug can bind to many similar targets and have different functional outcomes will inform drug design with desired efficacy profiles.

Original languageEnglish
Pages (from-to)719-730.e14
JournalCell
Volume172
Issue number4
DOIs
StatePublished - Feb 8 2018

Keywords

  • GPCR
  • crystal structures
  • ergotamine
  • polypharmacology
  • ritanserin
  • selectivity
  • serotonin 2C receptor

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