National Health and Medical Research Council (NHMRC, Australia)
1126857
Australia
National Health and Medical Research Council (NHMRC, Australia)
1184726
Australia
National Health and Medical Research Council (NHMRC, Australia)
1160076
Australia
National Health and Medical Research Council (NHMRC, Australia)
1150083
Australia
Japan Science and Technology
18069571
Japan
Citation
Journal: Cell Rep / Year: 2021 Title: Structure and dynamics of semaglutide- and taspoglutide-bound GLP-1R-Gs complexes. Authors: Xin Zhang / Matthew J Belousoff / Yi-Lynn Liang / Radostin Danev / Patrick M Sexton / Denise Wootten / Abstract: The glucagon-like peptide-1 receptor (GLP-1R) regulates insulin secretion, carbohydrate metabolism, and appetite and is an important target for treatment of type 2 diabetes and obesity. Multiple GLP- ...The glucagon-like peptide-1 receptor (GLP-1R) regulates insulin secretion, carbohydrate metabolism, and appetite and is an important target for treatment of type 2 diabetes and obesity. Multiple GLP-1R agonists have entered into clinical trials, with some, such as semaglutide, progressing to approval. Others, including taspoglutide, failed due to the high incidence of side effects or insufficient efficacy. GLP-1R agonists have a broad spectrum of signaling profiles, but molecular understanding is limited by a lack of structural information on how different agonists engage with the GLP-1R. Here, we report cryoelectron microscopy (cryo-EM) structures and cryo-EM 3D variability analysis of semaglutide- and taspoglutide-bound GLP-1R-Gs protein complexes. These reveal similar peptide interactions to GLP-1 but different motions within the receptor and bound peptides, providing insights into the molecular determinants of GLP-1R peptide engagement.
History
Deposition
Oct 22, 2020
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Header (metadata) release
Aug 4, 2021
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Map release
Aug 4, 2021
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Update
Aug 4, 2021
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Current status
Aug 4, 2021
Processing site: RCSB / Status: Released
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Structure visualization
Movie
Surface view with section colored by density value
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