Rhodopsin forms a dimer with cytoplasmic helix 8 contacts in native membranes

Biochemistry. 2012 Mar 6;51(9):1819-21. doi: 10.1021/bi3001598. Epub 2012 Feb 27.


G protein-coupled receptors form dimers and higher-order oligomers in membranes, but the precise mode of receptor-receptor interaction remains unknown. To probe the intradimeric proximity of helix 8 (H8), we conducted chemical cross-linking of endogenous cysteines in rhodopsin in disk membranes. We identified a Cys316-Cys316 cross-link using partial proteolysis and liquid chromatography with mass spectrometry. These results show that a symmetric dimer interface mediated by H1 and H8 contacts is present in native membranes.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Binding Sites
  • Cell Membrane / metabolism*
  • Chromatography, Liquid
  • Cysteine / chemistry
  • Cysteine / genetics
  • Cytoplasm / metabolism*
  • Dimerization
  • Mass Spectrometry
  • Protein Structure, Secondary
  • Proteolysis
  • Rhodopsin / chemistry*
  • Rhodopsin / metabolism


  • Rhodopsin
  • Cysteine