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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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
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/3203b4bbea3845c690168fa0775d64d9
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spelling	oai:doaj.org-article:3203b4bbea3845c690168fa0775d64d92021-12-02T17:32:59ZFull-length human GLP-1 receptor structure without orthosteric ligands10.1038/s41467-020-14934-52041-1723https://doaj.org/article/3203b4bbea3845c690168fa0775d64d92020-03-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-14934-5https://doaj.org/toc/2041-1723Glucagon-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.Fan WuLinlin YangKaini HangMette LaursenLijie WuGye Won HanQiansheng RenNikolaj Kulahin RoedGuangyao LinMichael A. HansonHualiang JiangMing-Wei WangSteffen Reedtz-RungeGaojie SongRaymond C. StevensNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-10 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q 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 Full-length human GLP-1 receptor structure without orthosteric ligands
description	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.
format	article
author	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
author_facet	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
author_sort	Fan Wu
title	Full-length human GLP-1 receptor structure without orthosteric ligands
title_short	Full-length human GLP-1 receptor structure without orthosteric ligands
title_full	Full-length human GLP-1 receptor structure without orthosteric ligands
title_fullStr	Full-length human GLP-1 receptor structure without orthosteric ligands
title_full_unstemmed	Full-length human GLP-1 receptor structure without orthosteric ligands
title_sort	full-length human glp-1 receptor structure without orthosteric ligands
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/3203b4bbea3845c690168fa0775d64d9
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Full-length human GLP-1 receptor structure without orthosteric ligands

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