H. E. Xu

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 identifies a conserved binding pocket in class B GPCRs that enables small molecule agonists like PCO371 to activate G proteins without triggering arrestin signaling.

The paper reports the structure of NTSR1 bound to GRK2, Gq, and a biased ligand, revealing how the ligand enhances GRK2 binding and enables arrestin-biased signaling.

The paper presents cryo-EM structures of bombesin receptors bound to their neuropeptide ligands, revealing the mechanism of ligand selectivity and receptor activation for itch treatment.

The paper reports cryo-EM structures of PTH1R bound to PTH and PTHrP, revealing molecular mechanisms of hormone recognition and selectivity.

This study reports cryo-EM structures of all human dopamine receptor subtypes bound to Rotigotine, revealing binding modes, activation mechanisms, and G-protein coupling specificity for drug design.

The paper reports cryo-EM structures of FSHR in inactive and active states, revealing a conserved activation mechanism and the role of H6157.42 in agonist selectivity.

This study investigates the structural and biochemical features of Omicron BA.1 and BA.2 variants, showing increased infectivity and mouse ACE2 binding compared to wildtype, suggesting a potential human-cat-mouse-human transmission cycle.

This study reports cryo-EM structures of NMUR1 and NMUR2 bound to NMU and NMS, revealing peptide selectivity mechanisms and activation principles for drug design.

The paper presents cryo-EM structures of MC1R-Gs complexes with ligands, revealing calcium's role in hormone recognition and Gβ interactions, and a conserved activation mechanism.

The paper presents cryo-EM structures of the ghrelin receptor bound to ghrelin and GHRP-6, revealing the binding pocket for the octanoyl group and providing insights for drug design.

This study reports the cryo-EM structure of PTH2R bound to TIP39 and a Gs protein, revealing ligand specificity and disease-associated mutation effects.

This study determines the cryo-EM structure of the 5-HT1F receptor complex with lasmiditan and a G protein, revealing the mechanism of selective activation and informing drug design.

The paper reports structures of bradykinin receptors bound to their ligands and reveals mechanisms of selectivity and activation, providing insights for drug design.

The paper reports crystal and cryo-EM structures of human CCKAR and CCKBR with ligands, revealing ligand recognition and activation mechanisms.

The paper presents cryo-EM structures of CCKAR with different G proteins to elucidate its G protein coupling promiscuity and ligand recognition mechanism.

The paper determines the structure of the V2 vasopressin receptor bound to AVP and Gs, revealing how AVP activates the receptor and providing insights for drug design.

The paper reports cryo-EM structures of SARS-CoV-2 RdRp with nucleoside inhibitors, revealing their mechanism and guiding the design of more potent derivatives.

The paper determines the structure of SARS-CoV-2 Mpro and shows how GC376 inhibits its catalytic site, supporting its use as an antiviral drug.

This paper investigates how fentanyl activates the mu-opioid receptor through beta-arrestin biased signaling using molecular dynamics simulations and validates findings with synthesized compounds.

The paper reports the structure of arrestin-2 bound to neurotensin receptor 1, revealing a novel orientation that enables coupling to GPCRs lacking a C-terminal tail.