Rearrangement of the transmembrane domain interfaces associated with the activation of a GPCR hetero-oligomer
G protein-coupled receptors (GPCRs), such as GABAB, can integrate extracellular signals via allosteric interactions within dimers and oligomers. Here authors use crosslinking and identify two transmembrane interfaces in GABAB which undergo a concerted rearrangement upon agonist activation.
Guardado en:
Autores principales: | Li Xue, Qian Sun, Han Zhao, Xavier Rovira, Siyu Gai, Qianwen He, Jean-Philippe Pin, Jianfeng Liu, Philippe Rondard |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2019
|
Materias: | |
Acceso en línea: | https://doaj.org/article/2a62f546d82a4973a65a19204b56e900 |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
Ejemplares similares
-
Allosteric modulators enhance agonist efficacy by increasing the residence time of a GPCR in the active state
por: Anne-Marinette Cao, et al.
Publicado: (2021) -
Correction: Corrigendum: Conformational rearrangements in the transmembrane domain of CNGA1 channels revealed by single-molecule force spectroscopy
por: Sourav Maity, et al.
Publicado: (2017) -
Hetero-oligomer of dynamin-related proteins participates in the fission of highly divergent mitochondria from Entamoeba histolytica
por: Takashi Makiuchi, et al.
Publicado: (2017) -
Isolated Toll-like receptor transmembrane domains are capable of oligomerization.
por: James I Godfroy, et al.
Publicado: (2012) -
Swapping of transmembrane domains in the epithelial calcium channel TRPV6
por: Appu K. Singh, et al.
Publicado: (2017)