Structural determinants of 5-HT2Breceptor activation and biased agonism.
McCorvy, J.D., Wacker, D., Wang, S., Agegnehu, B., Liu, J., Lansu, K., Tribo, A.R., Olsen, R.H.J., Che, T., Jin, J., Roth, B.L.(2018) Nat Struct Mol Biol 25: 787-796
- PubMed: 30127358 
- DOI: https://doi.org/10.1038/s41594-018-0116-7
- Primary Citation of Related Structures:  
6DRX, 6DRY, 6DRZ, 6DS0 - PubMed Abstract: 
Serotonin (5-hydroxytryptamine; 5-HT) receptors modulate a variety of physiological processes ranging from perception, cognition and emotion to vascular and smooth muscle contraction, platelet aggregation, gastrointestinal function and reproduction. Drugs that interact with 5-HT receptors effectively treat diseases as diverse as migraine headaches, depression and obesity. Here we present four structures of a prototypical serotonin receptor-the human 5-HT 2B receptor-in complex with chemically and pharmacologically diverse drugs, including methysergide, methylergonovine, lisuride and LY266097. A detailed analysis of these structures complemented by comprehensive interrogation of signaling illuminated key structural determinants essential for activation. Additional structure-guided mutagenesis experiments revealed binding pocket residues that were essential for agonist-mediated biased signaling and ¦Â-arrestin2 translocation. Given the importance of 5-HT receptors for a large number of therapeutic indications, insights derived from these studies should accelerate the design of safer and more effective medications.
Organizational Affiliation: 
National Institute of Mental Health Psychoactive Drug Screening Program, Department of Pharmacology and Division of Chemical Biology and Medicinal Chemistry, University of North Carolina Chapel Hill Medical School, Chapel Hill, NC, USA. jmccorvy@mcw.edu.