Shining a light on GPCR complexes

J Biol Chem. 2017 Aug 25;292(34):14290-14291. doi: 10.1074/jbc.H117.797100.

Abstract

The G protein-coupled receptor (GPCR) signaling pathways mediating information exchange across the cell membrane are central to a variety of biological processes and therapeutic strategies, but visualizing the molecular-level details of this exchange has been difficult for all but a few GPCR-G protein complexes. A study by Gao et al. now reports new strategies and tools to obtain receptor complexes in a near-native state, revealing insights into the gross conformational features of rhodopsin-transducin interactions and setting the stage for future studies.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Eye Proteins / chemistry
  • Eye Proteins / metabolism*
  • GTP-Binding Protein beta Subunits / chemistry
  • GTP-Binding Protein beta Subunits / metabolism*
  • GTP-Binding Protein gamma Subunits / chemistry
  • GTP-Binding Protein gamma Subunits / metabolism*
  • Humans
  • Models, Molecular*
  • Protein Interaction Domains and Motifs / radiation effects
  • Protein Multimerization / radiation effects
  • Rhodopsin / chemistry
  • Rhodopsin / metabolism*
  • Rod Cell Outer Segment / enzymology
  • Rod Cell Outer Segment / metabolism
  • Rod Cell Outer Segment / radiation effects
  • Transducin / chemistry
  • Transducin / metabolism*

Substances

  • Eye Proteins
  • GTP-Binding Protein beta Subunits
  • GTP-Binding Protein gamma Subunits
  • Rhodopsin
  • Transducin