Cargando…
Rearrangement of the transmembrane domain interfaces associated with the activation of a GPCR hetero-oligomer
G protein-coupled receptors (GPCRs) can integrate extracellular signals via allosteric interactions within dimers and higher-order oligomers. However, the structural bases of these interactions remain unclear. Here, we use the GABA(B) receptor heterodimer as a model as it forms large complexes in th...
Autores principales: | Xue, Li, Sun, Qian, Zhao, Han, Rovira, Xavier, Gai, Siyu, He, Qianwen, Pin, Jean-Philippe, Liu, Jianfeng, Rondard, Philippe |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6591306/ https://www.ncbi.nlm.nih.gov/pubmed/31235691 http://dx.doi.org/10.1038/s41467-019-10834-5 |
Ejemplares similares
-
Allosteric ligands control the activation of a class C GPCR heterodimer by acting at the transmembrane interface
por: Liu, Lei, et al.
Publicado: (2021) -
Case study on the evolution of hetero-oligomer interfaces based on the differences in paralogous proteins
por: Aoto, Saki, et al.
Publicado: (2015) -
GPCR oligomers in pharmacology and signaling
por: González-Maeso, Javier
Publicado: (2011) -
Allosteric modulators enhance agonist efficacy by increasing the residence time of a GPCR in the active state
por: Cao, Anne-Marinette, et al.
Publicado: (2021) -
Stepwise design of pseudosymmetric protein hetero-oligomers
por: Kibler, Ryan D., et al.
Publicado: (2023)