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.

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Detalles Bibliográficos
Autores principales: 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
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/3203b4bbea3845c690168fa0775d64d9
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Sumario: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.