"Rasmussen, S. G. F. et al. Crystal structure of the 2 adrenergic receptorGs protein complex. Nature 477, 549555 (2011). Article ADS CAS PubMed PubMed Central Google Scholar Kang, Y. et al. Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser. Nature 523, 561567 (2015). Article ADS CAS PubMed PubMed Central Google Scholar Zhang, Y. et al. Cryo-EM structure of the activated GLP-1 receptor in complex with a G protein. Nature 546, 248253 (2017)."
"Liang, Y.-L. et al. Phase-plate cryo-EM structure of a class B GPCRG-protein complex. Nature 546, 118123 (2017). Article ADS CAS PubMed PubMed Central Google Scholar Chen, K. et al. Tail engagement of arrestin at the glucagon receptor. Nature 620, 904910 (2023). Article ADS CAS PubMed PubMed Central Google Scholar Shen, C. et al. Structural basis of GABAB receptorGi protein coupling. Nature 594, 594598 (2021)."
High-resolution structures of GPCRs bound to G proteins and arrestins have elucidated activation and coupling mechanisms across class A and B receptors. Cryo-EM and femtosecond X-ray methods captured active and inactive states, revealing tail engagement, transducer specificity, and allosteric sites. Structural insights enable rational design of biased ligands, modality-selective agents, and novel indications. Genetic analyses identify GPCR variants linked to disease, informing precision therapies. Emerging platforms and structural pharmacology accelerate discovery of new agents and targets with improved efficacy and safety profiles. Integrated structural, genetic, and pharmacological data guide target selection, biomarker development, and translational strategies.
Read at www.nature.com
Unable to calculate read time
Collection
[
|
...
]