4L6R : Structure of the class B human glucagon G protein coupled receptor

  • Chris De Graaf (Contributor)
  • Dehua Yang (Contributor)
  • Chris De Graaf (Contributor)
  • Fai Yiu Siu (Contributor)
  • Ming Wei Wang (Contributor)
  • Ming Wei Wang (Contributor)
  • Vsevolod Katritch (Contributor)
  • Caihong Zhou (Contributor)
  • Ming Wei Wang (Contributor)
  • Gye Won Han (Contributor)
  • Chris De Graaf (Contributor)
  • Raymond C. Stevens (Contributor)
  • Gye Won Han (Contributor)
  • Chris De Graaf (Contributor)
  • Raymond C. Stevens (Contributor)
  • Raymond C. Stevens (Contributor)
  • Jesper Lau (Contributor)
  • Jesper Lau (Contributor)
  • Dehua Yang (Contributor)
  • Raymond C. Stevens (Contributor)
  • Vadim Cherezov (Contributor)
  • Dehua Yang (Contributor)
  • Ming Wei Wang (Contributor)
  • Ming Wei Wang (Contributor)
  • Ming Wei Wang (Contributor)
  • Vadim Cherezov (Contributor)
  • Vadim Cherezov (Contributor)
  • Wei Liu (Contributor)
  • Vsevolod Katritch (Contributor)
  • Raymond C. Stevens (Contributor)
  • Dehua Yang (Contributor)
  • Chris De Graaf (Contributor)
  • Dehua Yang (Contributor)
  • Raymond C. Stevens (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:3.3
Classification:MEMBRANE PROTEIN
Release Date:2013-07-24
Deposition Date:2013-06-12
Revision Date:2013-07-31#2013-08-07#2017-08-16#2017-11-15
Molecular Weight:48256.96
Macromolecule Type:Protein
Residue Count:425
Atom Site Count:3056
DOI:10.2210/pdb4l6r/pdb

Abstract:
Binding of the glucagon peptide to the glucagon receptor (GCGR) triggers the release of glucose from the liver during fasting; thus GCGR plays an important role in glucose homeostasis. Here we report the crystal structure of the seven transmembrane helical domain of human GCGR at 3.4 Å resolution, complemented by extensive site-specific mutagenesis, and a hybrid model of glucagon bound to GCGR to understand the molecular recognition of the receptor for its native ligand. Beyond the shared seven transmembrane fold, the GCGR transmembrane domain deviates from class A G-protein-coupled receptors with a large ligand-binding pocket and the first transmembrane helix having a 'stalk' region that extends three alpha-helical turns above the plane of the membrane. The stalk positions the extracellular domain (~12 kilodaltons) relative to the membrane to form the glucagon-binding site that captures the peptide and facilitates the insertion of glucagon's amino terminus into the seven transmembrane domain.
Date made availableJul 24 2013
PublisherRCSB-PDB

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