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Cell Research

Cell Research

IF: 25.9
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A unique hormonal recognition feature of the human glucagon-like peptide-2 receptor

Published:25 November 2020 DOI: 10.1038/s41422-020-00442-0 PMID: 33239759
Wen Sun, Li-Nan Chen, Qingtong Zhou, Li-Hua Zhao, Dehua Yang, Huibing Zhang, Zhaotong Cong, Dan-Dan Shen, Fenghui Zhao, Fulai Zhou, Xiaoqing Cai, Yan Chen, Yan Zhou, Sarina Gadgaard, Wijnand J. C. van der Velden, Suwen Zhao, Yi Jiang, Mette M. Rosenkilde, H. Eric Xu, Yan Zhang, Ming-Wei Wang

Abstract

Glucagon-like peptides (GLP-1 and GLP-2) are two proglucagon-derived intestinal hormones that mediate distinct physiological functions through two related receptors (GLP-1R and GLP-2R) which are important drug targets for metabolic disorders and Crohn’s disease, respectively. Despite great progress in GLP-1R structure determination, our understanding on the differences of peptide binding and signal transduction between these two receptors remains elusive. Here we report the electron microscopy structure of the human GLP-2R in complex with GLP-2 and a Gs heterotrimer. To accommodate GLP-2 rather than GLP-1, GLP-2R fine-tunes the conformations of the extracellular parts of transmembrane helices (TMs) 1, 5, 7 and extracellular loop 1 (ECL1). In contrast to GLP-1, the N-terminal histidine of GLP-2 penetrates into the receptor core with a unique orientation. The middle region of GLP-2 engages with TM1 and TM7 more extensively than with ECL2, and the GLP-2 C-terminus closely attaches to ECL1, which is the most protruded among 9 class B G protein-coupled receptors (GPCRs). Functional studies revealed that the above three segments of GLP-2 are essential for GLP-2 recognition and receptor activation, especially the middle region. These results provide new insights into the molecular basis of ligand specificity in class B GPCRs and may facilitate the development of more specific therapeutics.

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