Structure of rhodopsin and the superfamily of seven-helical receptors: the same and not the same

Curr Opin Cell Biol. 2002 Apr;14(2):189-95. doi: 10.1016/s0955-0674(02)00306-x.

Abstract

The crystal structure of rhodopsin provides significant insights concerning structure/activity relationships in visual pigments and related G-protein-coupled receptors. The specific arrangement of seven-transmembrane helices is stabilized by a series of intermolecular interactions that appear to be conserved among Family A receptors. However, the potential for structural and functional diversity among members of the superfamily of seven-helical receptors presents a significant future challenge.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • GTP-Binding Proteins / metabolism*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Retinoids / chemistry
  • Rhodopsin / chemistry*
  • Rhodopsin / metabolism
  • Structure-Activity Relationship

Substances

  • Retinoids
  • retinylidene chromophore
  • Rhodopsin
  • GTP-Binding Proteins