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TitleA unique hormonal recognition feature of the human glucagon-like peptide-2 receptor.
Journal, issue, pagesCell Res, Vol. 30, Issue 12, Page 1098-1108, Year 2020
Publish dateNov 25, 2020
AuthorsWen 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 /
PubMed AbstractGlucagon-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 ...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 G 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.
External linksCell Res / PubMed:33239759 / PubMed Central
MethodsEM (single particle)
Resolution3.0 Å
Structure data

30590

7d68

EMDB-30590, PDB-7d68:
Cryo-EM structure of the human glucagon-like peptide-2 receptor-Gs protein complex
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • bos taurus (cattle)
  • synthetic construct (others)
  • homo sapiens (human)
KeywordsBIOSYNTHETIC PROTEIN / Glucagon-like peptide-2 receptor / Drug target / Class B GPCR

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