Qingning Yuan

This study fine-tunes an intracellular allosteric pocket of NTSR1 to program GPCR signaling bias, revealing how ligand modifications alter transducer coupling and downstream signaling.

This study shows β-arrestin1 directly binds Gαs to sustain endosomal GPCR signaling by stabilizing Gs in a signaling-competent state.

This study determines the cryo-EM structures of OXGR1 bound to metabolites, revealing conserved mechanisms for metabolite recognition and receptor activation.

This study presents cryo-EM structures of hURAT1 bound with anti-gout drugs and uric acid, revealing transport mechanisms and drug inhibition.

The paper solves the cryo-EM structure of CCR1-Gi complex in pre-coupled state, revealing molecular mechanism of GPCR-G protein activation and highlighting conserved pre-coupling in chemokine receptors.

This study determines the cryo-EM structure of QRFPR bound to 26RFa, revealing the recognition mechanism and aiding drug design for obesity and diabetes.

This study presents cryo-EM structures of MCH-activated MCHR1 and MCHR2 with G-proteins, revealing ligand recognition mechanisms and activation pathways.

The paper presents cryo-EM structures of endothelin receptors bound to ligands, revealing their recognition mode and activation mechanism.

The paper reports the structures of TSHR activated by TSH and an autoantibody, revealing a universal activation mechanism and the role of cholesterol in TSHR localization.