Mechanochemical Activation of Class-B G-Protein-Coupled Receptor upon Peptide-Ligand Binding.

Atomic force microscopy G-protein-coupled receptors human glucagon receptor mechanotransduction single-molecule force spectroscopy

Journal

Nano letters
ISSN: 1530-6992
Titre abrégé: Nano Lett
Pays: United States
ID NLM: 101088070

Informations de publication

Date de publication:
08 07 2020
Historique:
pubmed: 25 6 2020
medline: 25 6 2021
entrez: 25 6 2020
Statut: ppublish

Résumé

Glucagon binding to the class-B G-protein-coupled glucagon receptor (GCGR) triggers the release of glucose from the liver during fasting. Recently, GCGR crystal structures have highlighted the conformation and molecular details of inactive and active receptor states. However, the dynamics of the conformational changes accompanying GCGR activation remains unclear. Here, we use multiplex force-distance curve-based atomic force microscopy (FD-based AFM) to probe

Identifiants

pubmed: 32578992
doi: 10.1021/acs.nanolett.0c02333
doi:

Substances chimiques

Ligands 0
Peptides 0
Receptors, G-Protein-Coupled 0

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

5575-5582

Auteurs

Cristina Lo Giudice (C)

Louvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.

Haonan Zhang (H)

CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.

Beili Wu (B)

CAS Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai, China.

David Alsteens (D)

Louvain Institute of Biomolecular Science and Technology, Université Catholique de Louvain, Louvain-la-Neuve, Belgium.

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Classifications MeSH