Structural origins of constitutive activation in rhodopsin: Role of the K296/E113 salt bridge.

@article{Kim2004StructuralOO,
  title={Structural origins of constitutive activation in rhodopsin: Role of the K296/E113 salt bridge.},
  author={J M Kim and Christian Altenbach and Masahiro Kono and Daniel D Oprian and Wayne L. Hubbell and Har Gobind Khorana},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2004},
  volume={101 34},
  pages={12508-13}
}
The intramolecular interactions that stabilize the inactive conformation of rhodopsin are of primary importance in elucidating the mechanism of activation of this and other G protein-coupled receptors. In the present study, site-directed spin labeling is used to explore the role of a buried salt bridge between the protonated Schiff base at K296 in TM7 and its counterion at E113 in TM3. Spin-label sensors are placed at positions in the cytoplasmic surface of rhodopsin to monitor changes in the… CONTINUE READING

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