August 2022 GPCRs steer G i and G s selectivity via TM5-TM6 switches as revealed by structures of serotonin The structural basis for G protein subtype selectivity by these GPCRs remains elusive. Here, we report the structures of the serotonin receptors 5-HT4, 5-HT6, and 5-HT7 with Gs, and 5-HT4 The structures reveal that transmembrane helices TM5 and TM6 alternate lengths as a macro-switch to determine We find that the macro-switch by the TM5-TM6 length is shared by class A GPCR-G protein structures.

August 2022 "Single particle cryogenic-electron microscopy (cryo-EM) is used extensively to determine structures of activated G protein-coupled receptors (GPCRs) in complex with G proteins or arrestins. Although a similar strategy has the potential to broadly facilitate cryo-EM structure determination of Here, we address this shortcoming by exploring different fusion protein designs, which lead to structures The fusion strategies explored here are likely applicable to cryo-EM interrogation of other GPCRs and

Here, we report the cryo-EM structures of an EBI2-Gi signaling complex with its endogenous agonist 7α These structures reveal an agonist binding site for the oxysterol and a potential ligand entrance site

< GPCR News < GPCRs in Oncology and Immunology Structural Basis for the Recognition of GPRC5D by Talquetamab Here, we elucidate the structure of GPRC5D complexed with the Fab fragment of talquetamab, using cryo-electron The structure offers insights for optimizing antibody design against GPRC5D for relapsed or refractory Junhyeon Park, Geun Young Mo, Jinwoo Shin, Yunje Cho Tags GPRC5D , Multiple myeloma , class C GPCR , cryo-EM structure , talquetamab Source Contribute to the GPCR News Coming soon Become a Contributor Classified

Committee Sponsors GPCR Retreat Program < Back to schedule Biased agonism at the GLP-1 receptor: from structure Patrick Sexton " Patrick Sexton is a NHMRC Senior Principal Research Fellow and Director, ARC Centre for Cryo-electron Recently, his team has applied cryo-EM to elucidation of the structure and dynamics of GPCRs. Prof.

using cryo-EM. Subsequent work has focused on understanding the molecular basis of GPCR pharmacology through structure In 2016 mini-G proteins were developed as a tool for the structure determination of GPCRs in the fully , and also by electron cryo-microscopy of receptors coupled to mini G protein bound to βγ subunits. to arrestin and also the first structure of a Class D receptor.