The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors

Annu Rev Biophys Biomol Struct. 2003:32:375-97. doi: 10.1146/annurev.biophys.32.110601.142520. Epub 2003 Feb 5.

Abstract

G protein-coupled receptors (GPCRs) are integral membrane proteins that respond to environmental signals and initiate signal transduction pathways activating cellular processes. Rhodopsin is a GPCR found in rod cells in retina where it functions as a photopigment. Its molecular structure is known from cryo-electron microscopic and X-ray crystallographic studies, and this has reshaped many structure/function questions important in vision science. In addition, this first GPCR structure has provided a structural template for studies of other GPCRs, including many known drug targets. After presenting an overview of the major structural elements of rhodopsin, recent literature covering the use of the rhodopsin structure in analyzing other GPCRs will be summarized. Use of the rhodopsin structural model to understand the structure and function of other GPCRs provides strong evidence validating the structural model.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Motifs
  • Cryoelectron Microscopy*
  • Crystallography / methods
  • Crystallography, X-Ray*
  • GTP-Binding Proteins / chemistry*
  • Macromolecular Substances
  • Models, Molecular*
  • Protein Binding
  • Protein Conformation
  • Protein Structure, Secondary
  • Rhodopsin / chemistry*

Substances

  • Macromolecular Substances
  • Rhodopsin
  • GTP-Binding Proteins