Skip to main content
FACULTY PROFILE STYLESHEET: do not remove this block

Roger Sunahara, Ph.D.

Professor of Pharmacology

George Chang, PhD

Research Interests

My laboratory primarily focuses on understanding the mechanism by which hormone binding to G protein-coupled receptors (GPCRs) lead to activation of signaling cascades. GPCRs are cell surface proteins that detect environmental stimuli and are key conduits for intracellular communication. This superfamily of genes (3rd largest in the human genome) contains members responsible for vision, smell and taste. Family members also serve as the primary receptors for hormones such as epinephrine, serotonin and dopamine, as well as chemokines, to name few. Following activation by this vast array of stimuli GPCRs couple to the heterotrimeric family of G proteins, intracellular proteins that serve as arbiters between the receptor and downstream effector such as adenylyl cyclase, phospholipase C and ion channels, to name a few. GPCRs continue to be the most popular targets for all therapeutics currently on the market, yet off-target activity, as well as our poor understanding for the structural basis of ligand efficacy, remain as major contributors to adverse reactions or side-effects.  My laboratory is keenly interested in the nature of the allosteric relationship between hormone binding and G protein activation. We utilize  biochemical, biophysical and pharmacological approaches to study how hormones and ligands influence receptor-G protein coupling and to understand the mechanisms underlying the implicit cooperativity. Achieving a better understanding of the structural and functional basis of this allostery will help us understand the mechanisms underlying ligand efficacy.  Together with structure-guided drug discovery initiatives we hope to use these models to develop safer and more efficacious therapeutics.


Selected Publications

Rasmussen SGF, et al. Crystal Structure of the β2 Adrenergic Receptor-Gs protein complex, Nature 2011 Jul 19;477(7366):549-55.

Chung KY et al. β2 adrenergic receptor-induced conformational changes in the heterotrimeric G protein Gs, Nature. 2011 Sep 28;477(7366):611-5.

Irannejad R et al, Conformational biosensors reveal adrenoceptor signaling from endosomes, Nature, Mar 28;495(7442):534-8, 2013.

Dror RO, et al, Structural basis for nucleotide exchange in heterotrimeric G proteins, Science. 2015 Jun 19;348(6241):1361-5. doi: 10.1126.

(DeVree BT, Mahoney JP, equal first) et al. Allosteric coupling from G protein to the agonist binding pocket in GPCRs. Nature, 2016 Jul 7;535(7610):182-6.

Yin J, et al.  Structure of a D2 dopamine receptor-G protein complex in a lipid membrane Nature 2020, Aug;584(7819):125-129. PMID: 32528175

 Maeda S, et al. Structure and selectivity engineering of the M1 muscarinic receptor toxin complex Science 2020, Jul 10;369(6500):161-167. PMID: 32646996

Huang SK, et al. Delineating the conformational landscape of the adenosine A2A receptor during G protein coupling.  Cell 2021 Apr 1;184(7):1884-1894. PMID: 33743210


Cancer Biology
Cardiovascular & Metabolic Diseases
Immunology, Inflammation, & Infectious Diseases
Neuropharmacology & Neurological Disorders


Signaling & Molecular Pharmacology
Biochemical, Biophysical and Structural Pharmacology


(858) 246-1967


UCSD Profile