Making Structural Sense of Dimerization Interfaces of Delta Opioid Receptor Homodimers†

@inproceedings{Johnston2011MakingSS,
  title={Making Structural Sense of Dimerization Interfaces of Delta Opioid Receptor Homodimers†},
  author={Jennifer M. Johnston and Mahalaxmi Aburi and Davide Provasi and Andrea Bortolato and Eneko Urizar and Nevin A. Lambert and Jonathan A. Javitch and Marta Filizola},
  booktitle={Biochemistry},
  year={2011}
}
Opioid receptors, like other members of the G protein-coupled receptor (GPCR) family, have been shown to associate to form dimers and/or oligomers at the plasma membrane. Whether this association is stable or transient is not known. Recent compelling evidence suggests that at least some GPCRs rapidly associate and dissociate. We have recently calculated binding affinities from free energy estimates to predict transient association between mouse delta opioid receptor (DOR) protomers at a… CONTINUE READING