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TitleConformational states of the full-length glucagon receptor.
Journal, issue, pagesNat Commun, Vol. 6, Page 7859, Year 2015
Publish dateJul 31, 2015
AuthorsLinlin Yang / Dehua Yang / Chris de Graaf / Arne Moeller / Graham M West / Venkatasubramanian Dharmarajan / Chong Wang / Fai Y Siu / Gaojie Song / Steffen Reedtz-Runge / Bruce D Pascal / Beili Wu / Clinton S Potter / Hu Zhou / Patrick R Griffin / Bridget Carragher / Huaiyu Yang / Ming-Wei Wang / Raymond C Stevens / Hualiang Jiang /
PubMed AbstractClass B G protein-coupled receptors are composed of an extracellular domain (ECD) and a seven-transmembrane (7TM) domain, and their signalling is regulated by peptide hormones. Using a hybrid ...Class B G protein-coupled receptors are composed of an extracellular domain (ECD) and a seven-transmembrane (7TM) domain, and their signalling is regulated by peptide hormones. Using a hybrid structural biology approach together with the ECD and 7TM domain crystal structures of the glucagon receptor (GCGR), we examine the relationship between full-length receptor conformation and peptide ligand binding. Molecular dynamics (MD) and disulfide crosslinking studies suggest that apo-GCGR can adopt both an open and closed conformation associated with extensive contacts between the ECD and 7TM domain. The electron microscopy (EM) map of the full-length GCGR shows how a monoclonal antibody stabilizes the ECD and 7TM domain in an elongated conformation. Hydrogen/deuterium exchange (HDX) studies and MD simulations indicate that an open conformation is also stabilized by peptide ligand binding. The combined studies reveal the open/closed states of GCGR and suggest that glucagon binds to GCGR by a conformational selection mechanism.
External linksNat Commun / PubMed:26227798 / PubMed Central
MethodsEM (single particle)
Resolution34.0 - 40.0 Å
Structure data

EMDB-6357:
Negative stain (RCT) surface of full-length glucagon receptor FAB complex
Method: EM (single particle) / Resolution: 34.0 Å

EMDB-6358:
Negative stain (RCT) surface of full-length glucagon receptor FAB complex
Method: EM (single particle) / Resolution: 40.0 Å

Source
  • Homo sapiens (human)
  • Mus musculus (house mouse)

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