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

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
Source :
Nature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
Publication Year :
2020
Publisher :
Nature Portfolio, 2020.

Abstract

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.

Subjects

Subjects :
Science

Details

Language :
English
ISSN :
20411723
Volume :
11
Issue :
1
Database :
Directory of Open Access Journals
Journal :
Nature Communications
Publication Type :
Academic Journal
Accession number :
edsdoj.3203b4bbea3845c690168fa0775d64d9
Document Type :
article
Full Text :
https://doi.org/10.1038/s41467-020-14934-5