U.S. Department of Health and Human Services
Jürgen Wess

 Contact Info

Tel: 301-402-3589
Email: jurgenw@helix.nih.gov

 Select Experience

  • ChiefMolecular Signaling Section, Laboratory of Biological Chemistry, NIDDK, NIH1998
  • HeadG Protein-Coupled Receptor Unit, NIDDK, NIH1993-1997
  • HeadG Protein-Coupled Receptor Unit, NINDS, NIH1991-1993
  • Postdoctoral FellowJoint Appointment at NIMH and NINDS, NIH1988-1991
  • Ph.D.Johann Wolfgang-Goethe University1987

 Related Links

  • Cell Biology/Cell Signaling
  • Molecular Biology/Biochemistry
  • Molecular Pharmacology/Toxicology

​Research Images

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Schematic representation of CNO-sensitive designer GPCRs (DREADDs)

All depicted DREADDs contain the Y3.33C and A5.46G point mutations in TM3 and TM5, respectively (indicated by the red 'x marks'). The resulting designer receptors are unable to bind acetylcholine (ACh), the endogenous muscarinic receptor agonist, but can be activated by CNO with high potency and efficacy. CNO is a pharmacologically inactive metabolite of clozapine. Depicted are (B) DREADDs differing in their G protein coupling properties (Armbruster BN, et al. Proc. Natl. Acad. Sci. U.S.A. 104, 5163-8, 2007; Guettier JM, et al. Proc. Natl. Acad. Sci. U.S.A. 106, 19197-19202, 2009) and (C) the structure of an arrestin-biased DREADD (Nakajima KI and Wess J. Mol. Pharmacol. 82, 575-82, 2012).

Schematic representation of CNO-sensitive designer GPCRs (DREADDs)Enlarge
Expression of a designer GPCR in mouse beta-cells

Selective expression of a Gq-coupled designer GPCR (Gq DREADD; DREAD, Designer Receptor Exclusively Activated by a Designer Drug) in pancreatic beta-cells of a transgenic mouse line

A graphic with a cartoon mouse, beta cell, and pancreas showing selective expression of a Gq-coupled designer GPCREnlarge
Wess Photo Lab Members(From left to right): Kelly Hu, Yinghong Cui, Derek Bone, Sally McMillin, Shalini Jain, Jürgen Wess, Mario Rossi, Ken-ichiro Nakajima, Wataru Sakamoto, and Jianxin HuWess Photo Lab MembersEnlarge
High-resolution X-ray structure of the M3 muscarinic receptor (M3R)(A) Overall structure of the M3R bound to tiotropium, a muscarinic antagonist used for the treatment of chronic obstructive pulmonary disease and (B) an extracellular view of the tiotropium binding site (Kruse AC, et al. Nature 482, 552-6, 2012).High-resolution X-ray structure of the M3 muscarinic receptor (M3R)Enlarge