Stability of dark state rhodopsin is mediated by a conserved ion pair in intradiscal loop E-2.

@article{Janz2003StabilityOD,
  title={Stability of dark state rhodopsin is mediated by a conserved ion pair in intradiscal loop E-2.},
  author={Jay M. Janz and Jonathan F Fay and David L. Farrens},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 19},
  pages={16982-91}
}
The rhodopsin crystal structure reveals that intradiscal loop E-2 covers the 11-cis-retinal, creating a "retinal plug." Recently, we noticed the ends of loop E-2 are linked by an ion pair between residues Arg-177 and Asp-190, near the highly conserved disulfide bond. This ion pair appears biologically significant; it is conserved in almost all vertebrate opsins and may occur in other G-protein-coupled receptors. We report here that the Arg-177/Asp-190 ion pair is critical for the folding and… CONTINUE READING

From This Paper

Topics from this paper.

Citations

Publications citing this paper.
Showing 1-10 of 26 extracted citations

Structure and activation of the visual pigment rhodopsin.

Annual review of biophysics • 2010
View 10 Excerpts
Highly Influenced

Evolution of nonspectral rhodopsin function at high altitudes.

Proceedings of the National Academy of Sciences of the United States of America • 2017

Lifting the lid on GPCRs: the role of extracellular loops.

British journal of pharmacology • 2012
View 2 Excerpts

Similar Papers

Loading similar papers…