Cargando…
Making Structural Sense of Dimerization Interfaces of Delta Opioid Receptor Homodimers
[Image: see text] 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...
Autores principales: | Johnston, Jennifer M., Aburi, Mahalaxmi, Provasi, Davide, Bortolato, Andrea, Urizar, Eneko, Lambert, Nevin A., Javitch, Jonathan A., Filizola, Marta |
---|---|
Formato: | Texto |
Lenguaje: | English |
Publicado: |
American Chemical Society
2011
|
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3050604/ https://www.ncbi.nlm.nih.gov/pubmed/21261298 http://dx.doi.org/10.1021/bi101474v |
Ejemplares similares
-
Lessons from Free Energy Simulations of δ-Opioid Receptor Homodimers Involving the Fourth Transmembrane Helix
por: Provasi, Davide, et al.
Publicado: (2010) -
Preferred Supramolecular Organization and Dimer Interfaces of Opioid Receptors from Simulated Self-Association
por: Provasi, Davide, et al.
Publicado: (2015) -
Molecular details of dimerization kinetics reveal negligible populations of transient µ-opioid receptor homodimers at physiological concentrations
por: Meral, Derya, et al.
Publicado: (2018) -
Assessing the Relative Stability of Dimer Interfaces in G Protein-Coupled Receptors
por: Johnston, Jennifer M., et al.
Publicado: (2012) -
Atomic-Level Characterization of the Methadone-Stabilized Active Conformation of µ-Opioid Receptor
por: Kapoor, Abhijeet, et al.
Publicado: (2020)