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TitleStructural and functional diversity among agonist-bound states of the GLP-1 receptor.
Journal, issue, pagesNat Chem Biol, Vol. 18, Issue 3, Page 256-263, Year 2022
Publish dateDec 22, 2021
AuthorsBrian P Cary / Giuseppe Deganutti / Peishen Zhao / Tin T Truong / Sarah J Piper / Xinyu Liu / Matthew J Belousoff / Radostin Danev / Patrick M Sexton / Denise Wootten / Samuel H Gellman /
PubMed AbstractRecent advances in G-protein-coupled receptor (GPCR) structural elucidation have strengthened previous hypotheses that multidimensional signal propagation mediated by these receptors depends, in ...Recent advances in G-protein-coupled receptor (GPCR) structural elucidation have strengthened previous hypotheses that multidimensional signal propagation mediated by these receptors depends, in part, on their conformational mobility; however, the relationship between receptor function and static structures is inherently uncertain. Here, we examine the contribution of peptide agonist conformational plasticity to activation of the glucagon-like peptide 1 receptor (GLP-1R), an important clinical target. We use variants of the peptides GLP-1 and exendin-4 (Ex4) to explore the interplay between helical propensity near the agonist N terminus and the ability to bind to and activate the receptor. Cryo-EM analysis of a complex involving an Ex4 analog, the GLP-1R and G heterotrimer revealed two receptor conformers with distinct modes of peptide-receptor engagement. Our functional and structural data, along with molecular dynamics (MD) simulations, suggest that receptor conformational dynamics associated with flexibility of the peptide N-terminal activation domain may be a key determinant of agonist efficacy.
External linksNat Chem Biol / PubMed:34937906 / PubMed Central
MethodsEM (single particle)
Resolution2.41 - 2.51 Å
Structure data

24805

7s1m

EMDB-24805, PDB-7s1m:
Ex4-D-Ala bound to the glucagon-like peptide-1 receptor/g protein complex (conformer 1)
Method: EM (single particle) / Resolution: 2.41 Å

24825

7s3i

EMDB-24825, PDB-7s3i:
Ex4-D-Ala bound to the glucagon-like peptide-1 receptor/g protein complex (conformer 2)
Method: EM (single particle) / Resolution: 2.51 Å

Source
  • homo sapiens (human)
  • lama glama (llama)
  • synthetic construct (others)
KeywordsMEMBRANE PROTEIN / glucagon / GLP-1 / exendin / G protein / GDP / GTP / complex / agonist / D-alanine / D-Ala / GLP-1R

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