Crystal structure of rhodopsin: a template for cone visual pigments and other G protein-coupled receptors

Biochim Biophys Acta. 2002 Oct 11;1565(2):168-82. doi: 10.1016/s0005-2736(02)00567-9.


The crystal structure of rhodopsin has provided the first three-dimensional molecular model for a G-protein-coupled receptor (GPCR). Alignment of the molecular model from the crystallographic structure with the helical axes seen in cryo-electron microscopic (cryo-EM) studies provides an opportunity to investigate the properties of the molecule as a function of orientation and location within the membrane. In addition, the structure provides a starting point for modeling and rational experimental approaches of the cone pigments, the GPCRs in cone cells responsible for color vision. Homology models of the cone pigments provide a means of understanding the roles of amino acid sequence differences that shift the absorption maximum of the retinal chromophore in the environments of different opsins.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Anura
  • Binding Sites
  • Cryoelectron Microscopy
  • Crystallography
  • Cytoplasm / chemistry
  • Humans
  • Membrane Proteins / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Receptors, Cell Surface / chemistry*
  • Retinal Cone Photoreceptor Cells / chemistry*
  • Retinal Pigments / chemistry*
  • Rhodopsin / chemistry*
  • Rod Opsins / chemistry


  • Membrane Proteins
  • Receptors, Cell Surface
  • Retinal Pigments
  • Rod Opsins
  • Rhodopsin

Associated data

  • PDB/1KPN
  • PDB/1KPW
  • PDB/1KPX