G protein-gated ion channel

Glucagon Receptor Structures Reveal G protein Specificity Mechanism

Retrieved on: 
Thursday, March 19, 2020

This study offers valuable insights into pleiotropic GPCR-G protein coupling and G protein specificity.

Key Points: 
  • This study offers valuable insights into pleiotropic GPCR-G protein coupling and G protein specificity.
  • Although GCGR couples to both G proteins through the common pocket, it does so with different interaction patterns, which account for G protein specificity.
  • Based on the structures of GCGR-G protein complexes, the researchers performed extensive functional studies using techniques such as mutagenesis, G protein activation and cell signaling to investigate the roles of key residues in the receptor-G protein binding interface in Gs and Gi activation.
  • The results show that conformational differences of intracellular loops and residue side chains in the receptor are sufficient to guide G protein selectivity.

Glucagon Receptor Structures Reveal G protein Specificity Mechanism

Retrieved on: 
Thursday, March 19, 2020

This study offers valuable insights into pleiotropic GPCR-G protein coupling and G protein specificity.

Key Points: 
  • This study offers valuable insights into pleiotropic GPCR-G protein coupling and G protein specificity.
  • Although GCGR couples to both G proteins through the common pocket, it does so with different interaction patterns, which account for G protein specificity.
  • Based on the structures of GCGR-G protein complexes, the researchers performed extensive functional studies using techniques such as mutagenesis, G protein activation and cell signaling to investigate the roles of key residues in the receptor-G protein binding interface in Gs and Gi activation.
  • The results show that conformational differences of intracellular loops and residue side chains in the receptor are sufficient to guide G protein selectivity.