The structure of mammalian rod opsins

Vision Res. 1984;24(11):1501-8. doi: 10.1016/0042-6989(84)90312-2.

Abstract

Ovine rhodopsin is organised in disc membranes as a monomer. The determination of its amino acid sequence has permitted the utilisation of structure prediction programmes which indicate the probable disposition of the polypeptide chain in the bilayer. This putative model is consistent with labelling data using the chemical probes, [14C]succinic anhydride, [125I]diazodiido sulphanilic acid and [125I]iodophenyl azide, and with the cleavage points for several proteases. More surprisingly the predicted structure points to the occurrence of breaks/distortions in the transmembrane helical segments. These distorted regions may be of primary functional importance to the protein and at least one is associated with the attachment point of the chromophore. This particular part of the structure is also identified as a "mutational hot spot", for bovine, equine, ovine and porcine opsins exhibit different sequences (but conserved molecular volumes) in the four residues following the retinyllysine. In an otherwise highly conserved protein with no obvious functional differences between the four species, the high substitution rate in this region is unexplained.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Membrane Proteins
  • Photoreceptor Cells / analysis*
  • Protein Conformation
  • Retinal Pigments*
  • Rhodopsin*
  • Sheep

Substances

  • Membrane Proteins
  • Retinal Pigments
  • Rhodopsin