Insights into congenital stationary night blindness based on the structure of G90D rhodopsin

EMBO Rep. 2013 Jun;14(6):520-6. doi: 10.1038/embor.2013.44. Epub 2013 Apr 12.


We present active-state structures of the G protein-coupled receptor (GPCRs) rhodopsin carrying the disease-causing mutation G90D. Mutations of G90 cause either retinitis pigmentosa (RP) or congenital stationary night blindness (CSNB), a milder, non-progressive form of RP. Our analysis shows that the CSNB-causing G90D mutation introduces a salt bridge with K296. The mutant thus interferes with the E113Q-K296 activation switch and the covalent binding of the inverse agonist 11-cis-retinal, two interactions that are crucial for the deactivation of rhodopsin. Other mutations, including G90V causing RP, cannot promote similar interactions. We discuss our findings in context of a model in which CSNB is caused by constitutive activation of the visual signalling cascade.

Publication types

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

MeSH terms

  • Arrestin / chemistry
  • Crystallography, X-Ray
  • Eye Diseases, Hereditary / genetics*
  • Genetic Diseases, X-Linked / genetics*
  • HEK293 Cells
  • Humans
  • Models, Molecular
  • Mutation, Missense*
  • Myopia / genetics*
  • Night Blindness / genetics*
  • Protein Binding
  • Protein Stability
  • Protein Structure, Secondary
  • Protein Structure, Tertiary
  • Rhodopsin / chemistry*
  • Rhodopsin / genetics
  • Schiff Bases
  • Structural Homology, Protein
  • Transition Temperature


  • Arrestin
  • Schiff Bases
  • Rhodopsin

Supplementary concepts

  • Night blindness, congenital stationary