The arrangement ok alpha helices in rhodopsin

G. F X Schertier*, V. M. Unger, P. A. Margrave, P. C. Edwards

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


Purpose: Determine the arrangement of helices of the G protein-coupled receptor Rhodopsin. Methods: Rhodopsins are the only seven helix receptors available in milligram quantities for crystallization. Electron cryo-microscopy of two dimensional crystals was used to determine the three dimensional structure of bovine and frog rhodopsin. Results: In the three dimensional map seven regions of density are visible from which tilt angles of all seven helices can be deduced. Conclusions: We have determined a medium resolution three dimensional structure of rhodopsin. The helices are tightly packed on the intracellular side. Towards the extracellular (i.e. intradiscal) side a cavity formed mainly from heiices 3,4,5,6 and 7 was observed which is most likely occupied by the retinal. The observed transmembrane structural features of rhodopsin are likely to represent a model for other G protein-coupled receptors.

Original languageEnglish (US)
Pages (from-to)A1295
JournalFASEB Journal
Issue number9
StatePublished - Dec 1 1997

ASJC Scopus subject areas

  • Biotechnology
  • Biochemistry
  • Molecular Biology
  • Genetics


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