Tao Che, Ph.D.
Assistant Professor
Anesthesiology
Biochemistry, Biophysics, and Structural Biology Program
Molecular Cell Biology Program
Neurosciences Program
314-446-8016
STLCOP, Academic Research Building, Rm. 614
taoche@wustl.edu
http://chelab.wustl.edu/
GPCRs, Analgesics, Side effects, opioid receptors, opioids, opioid alternatives
Characterizing and dissecting the molecular mechanisms of opioid receptor signaling
Research Abstract:
Research in the Che lab will be aimed at comprehensively characterizing and dissecting the molecular mechanisms of opioid receptor signaling. The goal is to gain an atomic-level understanding of opioid receptor activation, and to use this information to develop chemical and synthetic biologic tools (e.g., nanobodies) to ultimately lead to the development of safer, non-addictive pain medications. His work will integrate structural (e.g., X-ray, Cryo-EM) and pharmacological approaches, and leverage these data to generate subtype-specific novel chemicals as in vivo precision pharmacology probes to understand opioid receptor signaling spatiotemporally. These will be useful probes to interrogate signaling pathways and provide a platform for the discovery of new chemical and biological matter for potential therapeutic applications.
Selected Publications:
Che T, English J, Krumm BE, Kim K, Pardon E, Olsen RHJ, et al. Nanobody-enabled monitoring of kappa opioid receptor states. Nat Commun. 2020. PMID: 32123179.
Lyu JK, Wang S, Balius TE, Singh I, Levit A, Moroz YS, O’Meara MJ, Che T, Algaa E, Tolmachev AA, Shoichet BK, Roth BL & Irwin JJ. Ultra-large library docking for new chemotypes. Nature. 2019. PMID: 30728502.
Che T, Roth BL. Phosphoproteomics Illuminates Opioid Actions. Biochemistry. 2018. PMID: 30179451.
Wang S, Che T, Levit A, Shoichet BK, Wacker D, Roth BL. Structure of the D 2 dopamine receptor bound to the atypical antipsychotic drug risperidone. Nature. 2018 Mar 8;555(7695):269-273. PMID: 29466326.
Peng Y, McCorvy JD, Harpsøe K, Lansu K, Yuan S, Popov P, Qu L, Pu M, Che T, et al. 5-HT2C Receptor Structures Reveal the Structural Basis of GPCR Polypharmacology. Cell. 2018; PMID: 29398112.
Che T, Majumdar S, Zaidi SA, Ondachi P, McCorvy JD, Wang S, Mosier PD, et alL. Structure of the Nanobody-Stabilized Active State of the Kappa Opioid Receptor. Cell. 2018;172(1-2):55-67.
Last Updated: 6/5/2020 10:49:36 AM