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TitleDynamics of GLP-1R peptide agonist engagement are correlated with kinetics of G protein activation.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 92, Year 2022
Publish dateJan 10, 2022
AuthorsGiuseppe Deganutti / Yi-Lynn Liang / Xin Zhang / Maryam Khoshouei / Lachlan Clydesdale / Matthew J Belousoff / Hari Venugopal / Tin T Truong / Alisa Glukhova / Andrew N Keller / Karen J Gregory / Katie Leach / Arthur Christopoulos / Radostin Danev / Christopher A Reynolds / Peishen Zhao / Patrick M Sexton / Denise Wootten /
PubMed AbstractThe glucagon-like peptide-1 receptor (GLP-1R) has broad physiological roles and is a validated target for treatment of metabolic disorders. Despite recent advances in GLP-1R structure elucidation, ...The glucagon-like peptide-1 receptor (GLP-1R) has broad physiological roles and is a validated target for treatment of metabolic disorders. Despite recent advances in GLP-1R structure elucidation, detailed mechanistic understanding of how different peptides generate profound differences in G protein-mediated signalling is still lacking. Here we combine cryo-electron microscopy, molecular dynamics simulations, receptor mutagenesis and pharmacological assays, to interrogate the mechanism and consequences of GLP-1R binding to four peptide agonists; glucagon-like peptide-1, oxyntomodulin, exendin-4 and exendin-P5. These data reveal that distinctions in peptide N-terminal interactions and dynamics with the GLP-1R transmembrane domain are reciprocally associated with differences in the allosteric coupling to G proteins. In particular, transient interactions with residues at the base of the binding cavity correlate with enhanced kinetics for G protein activation, providing a rationale for differences in G protein-mediated signalling efficacy from distinct agonists.
External linksNat Commun / PubMed:35013280 / PubMed Central
MethodsEM (single particle)
Resolution3.3 - 3.7 Å
Structure data

23425

7lll

EMDB-23425, PDB-7lll:
Exendin-4-bound Glucagon-Like Peptide-1 (GLP-1) Receptor in complex with Gs protein
Method: EM (single particle) / Resolution: 3.7 Å

23436

7lly

EMDB-23436, PDB-7lly:
Oxyntomodulin-bound Glucagon-Like Peptide-1 (GLP-1) Receptor in complex with Gs protein
Method: EM (single particle) / Resolution: 3.3 Å

Source
  • homo sapiens (human)
  • lama glama (llama)
  • heloderma suspectum (Gila monster)
  • sus scrofa (pig)
KeywordsMEMBRANE PROTEIN / Glucagon-Like Peptide-1 (GLP-1) Receptor / extendin-4 / Oxyntomodulin

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