Asymmetry of the rhodopsin dimer in complex with transducin.

@article{Jastrzebska2013AsymmetryOT,
  title={Asymmetry of the rhodopsin dimer in complex with transducin.},
  author={Beata Jastrzebska and Tivadar Orban and Marcin Golczak and Andreas H. Engel and Krzysztof Palczewski},
  journal={FASEB journal : official publication of the Federation of American Societies for Experimental Biology},
  year={2013},
  volume={27 4},
  pages={1572-84}
}
A large body of evidence for G-protein-coupled receptor (GPCR) oligomerization has accumulated over the past 2 decades. The smallest of these oligomers in vivo most likely is a dimer that buries 1000-Å(2) intramolecular surfaces and on stimulation forms a complex with heterotrimeric G protein in 2:1 stoichiometry. However, it is unclear whether each of the monomers adopts the same or a different conformation and function after activation of this dimer. With bovine rhodopsin (Rho) and its… CONTINUE READING

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Stabilized G protein binding site in the structure of constitutively active metarhodopsin-II.

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