Full-length human GLP-1 receptor structure without orthosteric ligands

Glucagon-like peptide-1 receptor (GLP-1R) plays an important role in glucose homeostasis and treatment of type 2 diabetes. Here authors report the peptide-free crystal structure of human GLP-1R in an inactive state which reveals a unique closed conformation of the extracellular domain.

Bibliographic Details
Main Authors: Fan Wu, Linlin Yang, Kaini Hang, Mette Laursen, Lijie Wu, Gye Won Han, Qiansheng Ren, Nikolaj Kulahin Roed, Guangyao Lin, Michael A. Hanson, Hualiang Jiang, Ming-Wei Wang, Steffen Reedtz-Runge, Gaojie Song, Raymond C. Stevens
Format: Article
Language:English
Published: Nature Publishing Group 2020-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-020-14934-5
Description
Summary:Glucagon-like peptide-1 receptor (GLP-1R) plays an important role in glucose homeostasis and treatment of type 2 diabetes. Here authors report the peptide-free crystal structure of human GLP-1R in an inactive state which reveals a unique closed conformation of the extracellular domain.
ISSN:2041-1723